Use of aldh1a1 gene and protein in promoting hair follicle cell proliferation

Abstract

The application discloses ALDH1A1 The application discloses a gene and a protein in application of promoting hair follicle cell proliferation, and belongs to the technical field of functional gene application. ALDH1A1 The application discloses that overexpression of the gene can significantly promote hair follicle cell proliferation, and the ALDH1A1 protein is expected to be used for preparing a product for promoting hair follicle cell proliferation or damage repair, thereby providing a new and safe candidate preparation for improving the problem of hair loss. ALDH1A1 The application discloses that the expression amount of the gene in skin tissue is significantly higher than that in other tissues; compared with hair follicles in a regression period and a resting period, the expression amount of the gene in hair follicles in a growth period is the highest; and the structural and composition analysis results of the ALDH1A1 protein are provided.

Description

Technical Field

[0001] This invention relates to the field of functional gene application technology, and in particular to... ALDH1A1 Application of genes and proteins in promoting hair follicle cell proliferation. Background Technology

[0002] Cashmere goats are a globally important economic livestock, their core value lying in their cashmere—a natural protein fiber derived from secondary hair follicles in the skin. Due to its fineness, softness, warmth, moisture absorption, and breathability, it is known as "soft gold" and is a scarce raw material for the high-end textile industry. Cashmere goats have two types of wool: wool and cashmere. Their skin hair follicles consist of primary and secondary follicles. Primary follicles produce wool, primarily serving a protective function, while secondary follicles produce cashmere, providing warmth. Within each biological year, the growth and development of secondary follicles undergoes a cyclical process (divided into anagen (growth), catagen (transitional), and telogen (resting) phases, while primary follicles do not shed. The lengths of the anagen, catagen, and telogen phases of secondary hair follicles vary between breeds. For the Liaoning cashmere goat, a superior local breed in my country, the anagen phase of its secondary hair follicles is from April to October, the catagen phase from November to December, and the telogen phase from January to March. The periodic growth and development of secondary hair follicles is not only related to external factors such as light, temperature and humidity, but is also mainly regulated by internal signaling factors such as skin hair follicle-related genes and proteins.

[0003] acetaldehyde dehydrogenase 1A1 (ACED1A1) ALDH1A1 As an important member of the aldehyde dehydrogenase (ALDHs) superfamily, the ALDH gene is widely distributed in various tissues of organisms. Studies have shown that... ALDH1A1 It plays a role in the maintenance of nerve function, tumor development, tissue development, and lipid metabolism. Summary of the Invention

[0004] The purpose of this invention is to provide ALDH1A1 The application of genes and proteins in promoting hair follicle cell proliferation is disclosed for the first time in this invention by Liaoning cashmere goat. ALDH1A1 Information on the role of genes in promoting hair follicle cell proliferation and their protein composition and structural characteristics.

[0005] To achieve the above objectives, the present invention provides ALDH1A1 The application of genes in promoting hair follicle cell proliferation, the aforementioned ALDH1A1 The CDS sequence of the gene is shown in SEQ ID NO.3.

[0006] Include ALDH1A1 The application of gene vectors and engineered bacteria in the preparation of agents that promote hair follicle cell proliferation. ALDH1A1 The CDS sequence of the gene is shown in SEQ ID NO.3.

[0007] Preferably, the vector includes an overexpression vector.

[0008] Preferably, the engineered bacteria include recombinant Escherichia coli.

[0009] The application of ALDH1A1 protein in the preparation of agents that promote hair follicle cell proliferation, wherein the amino acid sequence of ALDH1A1 protein is shown in SEQ ID NO.4.

[0010] Preferably, the formulation uses ALDH1A1 protein as the active ingredient.

[0011] Preferably, the formulation includes shampoo and hair care products.

[0012] Therefore, the present invention provides ALDH1A1 The specific technical effects of using genes and proteins to promote hair follicle cell proliferation are as follows: (1) This invention is the first to discover overexpression ALDH1A1 The gene can significantly promote the proliferation of hair follicle cells. The ALDH1A1 protein is expected to be used to prepare products that promote the proliferation or repair of hair follicle cells, providing a new and safe candidate for improving hair loss problems. (2) This invention discloses Liaoning cashmere goat ALDH1A1 The gene was expressed at a significantly higher level in skin tissue than in other tissues; compared with telogen and catagen hair follicles, the gene was expressed at the highest level in anagen hair follicles; structural and compositional analysis of the ALDH1A1 protein was also provided.

[0013] The technical solution of the present invention will be further described in detail below with reference to the accompanying drawings and embodiments. Attached Figure Description

[0014] To more clearly illustrate the technical solutions of the embodiments of the present invention, the drawings used in the description of the embodiments of the present invention will be briefly introduced below. Obviously, the drawings described below are only some embodiments of the present invention. For those skilled in the art, other drawings can be obtained based on these drawings without creative effort.

[0015] Figure 1 This is an agarose gel electrophoresis image of the amplified product using cDNA as a template in Example 1 of this invention; Figure 2 The Liaoning cashmere goat in Embodiment 1 of this invention ALDH1A1 The sequencing results of the gene CDS and the goat in NCBI ALDH1A1 The results of the alignment of gene CDS; Figure 3 It is the evolutionary tree constructed in Embodiment 1 of the present invention; Figure 4 These are the structural prediction results of the ALDH1A1 protein in Example 2 of this invention; where A is the secondary structure prediction and B is the tertiary structure prediction. Figure 5 In different tissues in Embodiment 3 of the present invention ALDH1A1 Gene expression level analysis results; Figure 6 It is the skin at different times in Example 3 of the present invention ALDH1A1 Gene expression status; Figure 7 The three siRNA pairs in Example 4 of this invention ALDH1A1 Results of gene interference efficiency; Figure 8 This refers to the interference and overexpression in Embodiment 4 of the present invention. ALDH1A1 Post-CCK-8 results; where A represents the relative cell proliferation level after interference, and B represents the relative cell proliferation level after overexpression; Figure 9 This refers to the interference and overexpression in Embodiment 4 of the present invention. ALDH1A1 Post-EdU results; where A represents cells in the proliferative phase stained with EdU; B represents the EdU positivity rate after interference; and C represents the EdU positivity rate after overexpression. Figure 10 This refers to the interference and overexpression in Embodiment 4 of the present invention. ALDH1A1 The results of the cell colony formation ability test are shown in the figure below; where A is a plate colony image; B is the statistical result of the number of plate colonies after overexpression; and C is the statistical result of the number of plate colonies after interference. Detailed Implementation

[0016] The technical solution of the present invention will be further described below with reference to the accompanying drawings and embodiments.

[0017] To make the objectives, technical solutions, and advantages of this application clearer, more thorough, and more complete, the technical solutions of the present invention will be clearly and completely described below with reference to the accompanying drawings and embodiments. The following detailed descriptions are all illustrations of embodiments, intended to provide further detailed explanation of the present invention. Unless otherwise specified, all technical terms used in this invention have the same meaning as commonly understood by one of ordinary skill in the art to which this application pertains.

[0018] The instruments, equipment, reagents and materials used in the embodiments were all obtained through commercial means; the methods and steps not described in detail in the embodiments are all conventional techniques in the art.

[0019] Example 1 ALDH1A1 Gene cloning, specifically as follows: (1) Total RNA extraction. Three adult Liaoning cashmere goats of similar size and good health were randomly selected from the core breeding group of the Liaoning Academy of Animal Sciences. Skin samples (2cm×2cm) were surgically collected from both sides of the shoulder blades at three different times: March (resting period), September (growing period), and December (regression period). The three experimental goats were slaughtered, and tissues from the heart, liver, spleen, lungs, kidneys, and testes were collected, cut into 3-5cm strips, placed in cryovials, labeled, and then transported to the laboratory in liquid nitrogen for storage at -80℃ for subsequent experiments.

[0020] Take approximately 100 mg of skin tissue, add liquid nitrogen to an inactivated mortar, and grind the tissue sample into powder using a mortar and pestle before pouring it into an EP tube. Extract total RNA from the skin tissue of Liaoning cashmere goats according to the instructions provided with the RNA extraction kit.

[0021] (2) Preparation of cDNA. After determining the concentration of the prepared RNA solution using a spectrophotometer, reverse transcription was performed using a reverse transcription kit to convert the RNA into cDNA. The specific operation steps were performed according to the instructions accompanying the reverse transcription kit. The obtained cDNA was stored at -20℃ for later use.

[0022] (3) Design specific primers. Based on the data published in GenBank, goat... ALDH1A1 The gene sequence (accession number: XM_005683753.3) was used to design specific primers using Primer Premier 6.0 software, which were then synthesized by a company.

[0023] For ALDH1A1 The primers for gene cloning are shown in SEQ ID NO.1 and SEQ ID NO.2.

[0024] SEQ ID NO.1: ATGTCGTCCTCAGCCATGCC SEQ ID NO.2: TTATGAGTTCTGAGAAATTTTGAT (4) Using the cDNA synthesized in step (2) as a template, and the primers designed in step (3), amplify the cDNA using the Premix Taq kit. ALDH1A1 The complete CDS region of the gene was amplified using the following program: 94℃ pre-denaturation for 120 s; 94℃ denaturation for 30 s, 57℃ annealing for 30 s, 72℃ extension for 45 s, for a total of 34 cycles; 72℃ retrieval extension for 2 min; and storage at 4℃. 10 μL of the amplification product was subjected to 1% agarose gel electrophoresis, and the results are as follows. Figure 1 As shown, the bands were single and the size met expectations. The remaining amplified products were sent to the company for sequencing.

[0025] Sequencing results showed that the amplified fragment was 1506 bp in length, encoding 501 amino acids, consistent with the target fragment size and the expected result. (Liaoning cashmere goat) ALDH1A1 The CDS sequence of the gene is shown in SEQ ID NO.3, and the encoded amino acid sequence is shown in SEQ ID NO.4. The sequencing results were compared with those published by NCBI for goats. ALDH1A1 The gene CDS region sequence was compared, and the results are as follows: Figure 2 As shown, the sequencing results revealed a total of 18 base changes: C→G mutations at positions 33 and 34 bp, A→C mutation at position 36, A→G mutation at position 1085 bp, G→A mutation at position 1086 bp, G→C mutation at position 1112 bp, A→T mutation at position 1130 bp, G→A mutation at position 1135 bp, C→A mutation at position 1147 bp, T→C mutation at position 1160 bp, C→T mutation at position 1161 bp, T→C mutation at position 1162 bp, A→G mutation at position 1194 bp, G→A mutation at position 1195 bp, A→G mutation at position 1196 bp, G→A mutation at position 1198 bp, A→G mutation at position 1199 bp, and G→A mutation at position 1200 bp. Translation revealed that most of the above mutations were sense mutations, resulting in six amino acid changes in the ALDH1A1 protein: amino acid 250 changed from K (lysine) to S (serine), amino acid 251 changed from Y (tyrosine) to M (methionine), amino acid 252 changed from V (valine) to F (phenylalanine), amino acid 254 changed from G (glycine) to E (glutamic acid), and amino acid 255 changed from N (asparagine) to I (isoleucine).

[0026] SEQ ID NO.3: SEQ ID NO.4: MEAMNGGKLFSNAYLMDLGGCIKTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQIIPWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGSLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNAVEFAHQGVFYHQGQCC IAASRLFVEESIYDEFVRRSVERAKKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGRKEGAKLECAGGPWGIKSYFIKPTVSPDVTDDMRIAKRRIF GPVQQIMKFKSLDDVIKRANNTFYGLAAGIFTNDIDKAITVSSALQSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTIKISQKNS Liaoning cashmere goats ALDH1A1 The CDS region of the gene is associated with sheep, cattle, chickens, camels, red deer, pigs, zebu, and horses. ALDH1A1 Gene CDS region alignment results are shown in Table 1. The Liaoning cashmere goat shows high similarity to ruminants such as sheep, domestic cattle, red deer, and zebu, all exceeding 90%, indicating that... ALDH1A1 Genes are highly conserved among ruminants, with the lowest similarity found in the chicken species, at only 78.56%. A phylogenetic tree of these species was constructed using MEGA11 software, and the results are as follows: Figure 3 As shown.

[0027] Table 1 ALDH1A1 Similarity analysis results of gene CDS with other species

[0028] Example 2 Liaoning cashmere goats ALDH1A1 Bioinformatics analysis of genes is performed as follows: The physicochemical properties, signal peptide, transmembrane domain, phosphorylation site, glycosylation site, subcellular localization, secondary structure, and tertiary structure of the ALDH1A1 protein from Liaoning cashmere goat were predicted using various online bioinformatics analysis software. Interaction analysis of the ALDH1A1 protein was performed using the String interactive database. The URLs and functions of the software / databases used are shown in Table 2.

[0029] Table 2. Software / database URLs and functional information used.

[0030] (1) Physicochemical property analysis results show that the molecular formula of ALDH1A1 protein in Liaoning cashmere goat is C 2453 H 3838 N 648 O 727 S 24 The molecular weight is 54.80880 kDa, and the theoretical isoelectric point is 6.37. The amino acid composition is shown in Table 3, consisting of 501 amino acids. Glycine has the highest content (9.6%), and histidine has the lowest content (1.2%). There are 57 negatively charged amino acid residues (Asp+Glu) and 55 positively charged amino acid residues (Arg+Lys). Hydrophobic amino acids account for 45.4%, and the instability index is 33.06. The adipose coefficient is 80.58, the half-life is 30 h, and the predicted total average hydrophilicity of the protein is -0.170.

[0031] Table 3. Amino acid composition information of ALDH1A1 protein from Liaoning cashmere goat.

[0032] (2) The predicted structure of ALDH1A1 protein in Liaoning cashmere goat is as follows: Figure 4 As shown, the ALDH1A1 protein lacks a signal peptide sequence, has no transmembrane region, and contains 15 high-confidence phosphorylation sites (Score ≥ 0.5), namely 12 serine phosphorylation sites and 3 threonine phosphorylation sites. It has no O-glycosylation modification sites or N-glycosylation modification sites.

[0033] Secondary structure predictions showed that α-helices accounted for 42.14%, random coils for 31.07%, extended chains for 17.14%, and β-sheets for 9.64%. Figure 4 The prediction results for the tertiary structure and the secondary structure are consistent (A). Figure 4 B). Interaction analysis of the ALDH1A1 protein in Liaoning cashmere goat using the STRING interactive database showed that the ALDH1A1 protein interacts with ADH5 (alcohol dehydrogenase 5), CYP26A1, CYP26B1 (cytochrome), and RDH10 (retinol dehydrogenase 10) with high confidence (all scores ≥0.949).

[0034] Example 3 Liaoning cashmere goats ALDH1A1 Tissue-specific gene expression analysis was performed, as follows: (1) Primers for qRT-PCR were designed using the method described in part (3) of Example 1, with sequences shown in SEQ ID NO.5 and SEQ ID NO.6.β -actin is an internal reference gene, amplified... β The primer sequences for -actin are shown in SEQ ID NO.7 and SEQ ID NO.8.

[0035] SEQ ID NO.5: CATGGCGTATGGATGCTTCAG SEQ ID NO.6: CCACCATTCATAGCCTCCATTGTC SEQ ID NO.7: GGTGCCCATCTACGAGG SEQ ID NO.8: CTTGATTGTCACGGAGATT (2) Skin samples (2cm×2cm), heart, liver, spleen, lung, kidney, and testis tissues frozen in Example 1 were taken respectively. cDNA solutions of each tissue were obtained using the methods (1) and (2) of Example 1. The reaction system was prepared according to the instructions attached to the qRT-PCR. The qRT-PCR amplification program was: 95℃ pre-denaturation for 30s; 95℃ annealing for 10s; 60℃ extension for 20s, 40 cycles. Subsequently, the PCR products were analyzed by slowly increasing the temperature from 65℃ to 95℃ at a rate of 0.5℃ / 10s. The results are as follows. Figure 5 As shown, ALDH1A1 The gene is expressed in seven tissues: heart, liver, spleen, lung, kidney, testis, and skin. Among these, it is most prominent in skin tissue. ALDH1A1 The expression level of the gene was significantly higher than that of other tissues. P <0.01 indicates the dominant expression level of this gene in the tissues. The expression levels in the other six tissues, from highest to lowest, are spleen, kidney, testis, lung, liver, and heart, and the differences in expression levels among these tissues are statistically significant. P <0.01).

[0036] ALDH1A1 Expression patterns in the skin of Liaoning cashmere goats at different stages, as follows: Figure 6 As shown, ALDH1A1 The gene was expressed in the skin of Liaoning cashmere goats during the growth, regression, and resting phases, with the highest expression level during the growth phase (1.03±0.02), the lowest during the regression phase (0.34±0.02), and intermediate during the resting phase (0.71±0.04), showing a clear trend. The expression level during the growth phase was approximately three times that during the regression phase. P <0.01, which is 1.45 times the resting period ( P <0.05, the resting period is about twice the regression period ( P <0.05).

[0037] Example 4 Using immortalized secondary hair follicle stem cells from Liaoning cashmere goats as experimental material, the study investigated... ALDH1A1 The influence of genes on hair follicle stem cell proliferation was investigated. The method for constructing immortalized hair follicle stem cells from Liaoning cashmere goats was based on Hui Taiyu's (2025) doctoral dissertation at Shenyang Agricultural University, entitled "Study on the molecular mechanism of secondary hair follicle stem cell induction activation regulated by cashmere goat circRNA through m6A modification dependence". In this example, 9th generation secondary hair follicle stem cells were used, as detailed below: (1) Overexpression / interference experiment.

[0038] Construct three targeted goats ALDH1A1 The siRNA interference sequences of the gene (sequences shown in SEQ ID NO. 9-11) and a negative control (sequence shown in SEQ ID NO. 12) were sent to the company for synthesis. Then, using pcDNA3.1 as the backbone vector, a gene was constructed... ALDH1A1 Overexpression vector (recombinant overexpression vector).

[0039] SEQ ID NO.9: GAGUGGUAAGAAAUUUCCAGUCUUU SEQ ID NO.10: GACUGCUCUUCACAUGGGAUCUUUA SEQ ID NO.11: GGAACCGUGUGGGUGAACUGCUAUA SEQ ID NO.12: UUCUCCGAACGUGUCACGUTT The three siRNA interference sequences were transfected into cells and their expression was detected. The results are as follows: Figure 7 As shown, the interference efficiency is best with si-ALDH1A1-1, and the difference is extremely significant ( P With a concentration <0.01%, the efficiency can reach 71%. Therefore, the siRNA shown in SEQ ID NO.8 was selected for subsequent experiments.

[0040] (2) Cell viability was detected using the CCK8 assay, and the results are as follows: Figure 8 As shown in A, the cell viability of the interference group was significantly decreased ( P <0.01, the cell viability of the overexpression group increased significantly ( P <0.01), indicating ALDH1A1 Genes have a significant impact on the viability of secondary hair follicle stem cells. Interference and overexpression... ALDH1A1 The results of the relative viability assay of the cells after the experiment are as follows: Figure 8 As shown in B, in the interference group, compared with the si-NC control group, the relative viability of cells in the si-ALDH1A1 group was significantly higher at 24 h ( P The levels <0.05, 48h, and 72h were all significantly reduced (P <0.01) indicates a downward adjustment ALDH1A 1 expression significantly inhibited cell viability. In the overexpression group, compared with the pcDNA3.1-NC control group, the relative viability of cells in the OE-ALDH1A1 group was significantly increased at 24h, 48h, and 72h. P <0.01) indicates an upward adjustment ALDH1A1 Expression can significantly enhance cell viability.

[0041] (3) Hair follicle stem cell proliferation experiment.

[0042] 1) Co-culture of EdU and secondary hair follicle stem cells Secondary hair follicle stem cells, after being transfected with expression / interference (methods referencing Wang Niu's (2025) doctoral dissertation at Northwest A&F University, titled "Study on the Molecular Mechanism of FGF7 Regulating Hair Follicle Development in Goat") for 24 hours, were seeded into 24-well plates at a density of 1.5 × 10⁶ cells per well. 5 Cells were cultured normally for 24 hours to allow them to adhere. A preliminary experiment was conducted to determine the optimal EdU concentration as 10 nM and the incubation time as 2 hours. Cell samples without EdU were used as a negative control.

[0043] 2) Fixation and permeability.

[0044] After incubation, remove the culture medium. Add 1 mL of PBS containing 4% paraformaldehyde to each well and incubate at room temperature for 15 min to fix the cells. After discarding the waste liquid, add 1 mL of PBS containing 3% BSA to each well and wash thoroughly 3 times, 5 min each time. After discarding the waste liquid, add 1 mL of PBS containing 0.3% Triton X-100 to each well and incubate at room temperature for 20 min to permeate the cells.

[0045] 3) Fluorescent labeling.

[0046] After discarding the waste liquid, add 1 mL of PBS containing 3% BSA to each well and wash thoroughly three times, 5 min each time. Strictly follow the E-ClickEdU cell proliferation imaging assay kit (red, Elab Fluor). ® Prepare the Click reaction solution according to the instructions for 594 and use it within 15 minutes. After washing, add 250 μL of Click reaction solution to each well, gently shake to ensure the Click reaction solution evenly covers the cells, and incubate at room temperature in the dark for 30 minutes. Discard the supernatant, add 1 mL of PBS containing 3% BSA to each well and wash three times, 5 minutes each time.

[0047] 4) DNA staining and detection.

[0048] Discard the supernatant, add 500 μL of DAPI working solution to each well, and incubate at room temperature in the dark for 10 min. Discard the supernatant, add 1 mL of PBS containing 3% BSA to each well and wash three times, 5 min each time. To avoid fluorescence quenching, observe the results as soon as possible under a fluorescence microscope using an appropriate filter.

[0049] The results are as follows Figure 9 As shown, under a 10x magnification inverted fluorescence microscope, proliferating cells labeled with EdU are visible in each group. Compared with the si-NC control group, the interference... ALDH1A1 After expression of (si-ALDH1A1), the proportion of EdU-positive cells was significantly reduced; and compared with the pcDNA3.1-NC control group, overexpression... ALDH1A1 Following (OE-ALDH1A1) treatment, the proportion of EdU-positive cells significantly increased. Statistical analysis further confirmed that the proportion of EdU-positive cells in the interference group was significantly lower than that in the control group. P <0.01, while the proportion of EdU-positive cells in the overexpression group was significantly higher than that in the control group ( P <0.01). The above results indicate that... ALDH1A1 It can positively regulate the cell's DNA synthesis capacity, thereby promoting cell proliferation.

[0050] (2) Plate cloning experiment Secondary hair follicle stem cells transfected with expression / interference for 24 hours were seeded into 6-well plates, with 1000 cells per well. Each group had three replicates. The complete culture medium was changed every two days, and the cells were cultured for about one week until visible clones were observed. The old culture medium was discarded, and the cells were washed three times with 1 mL of PBS. 1 mL of 4% paraformaldehyde was added to each well for fixation for 30 min. The waste medium was discarded, and 1 mL of 0.1% crystal violet staining solution was added to each well. The cells were stained in the dark for 15 min, then washed several times with PBS. The clone count was then determined by photographing.

[0051] The results are as follows Figure 10 As shown, compared with the si-NC control group, the interference ALDH1A1 After expression of (si-ALDH1A1), the number of clones formed by the cells was significantly reduced. P <0.05); while compared with the pcDNA3.1 empty vector control group, overexpression ALDH1A1 After (OE-ALDH1A1), the number of clones formed by the cells increased significantly. P <0.01). The above results indicate that... ALDH1A1 The expression level of [a substance] was positively correlated with cell clonogenic ability, suggesting [a certain correlation]. ALDH1A1 It plays a positive promoting role in regulating cell proliferation and colony formation.

[0052] Therefore, this invention is the first to discover overexpression ALDH1A1The gene can significantly promote hair follicle cell proliferation. The ALDH1A1 protein holds promise for use in preparing products that promote hair follicle cell proliferation or damage repair, providing a new and highly safe candidate for improving hair loss problems; the gene from Liaoning cashmere goat is disclosed. ALDH1A1 The gene was expressed at a significantly higher level in skin tissue than in other tissues; compared with telogen and catagen hair follicles, the gene was expressed at the highest level in anagen hair follicles; structural and compositional analysis of the ALDH1A1 protein was also provided.

[0053] Finally, it should be noted that the above embodiments are only used to illustrate the technical solutions of the present invention and not to limit them. Although the present invention has been described in detail with reference to preferred embodiments, those skilled in the art should understand that modifications or equivalent substitutions can still be made to the technical solutions of the present invention, and these modifications or equivalent substitutions cannot cause the modified technical solutions to deviate from the spirit and scope of the technical solutions of the present invention.

Claims

1. ALDH1A1 The application of genes in promoting hair follicle cell proliferation is characterized by: The said ALDH1A1 The CDS sequence of the gene is shown in SEQ ID NO.

3.

2. Inclusion ALDH1A1 The application of a vector containing a gene and an engineered bacterium in the preparation of a preparation for promoting the proliferation of hair follicle cells, characterized in that: The ALDH1A1 CDS sequence of the gene is shown in SEQ ID NO.

3.

3. Use of the vector and engineered bacterium containing ALDH1A1 the gene in the preparation of a preparation for promoting the proliferation of hair follicle cells, characterized in that: The vector includes an overexpression vector.

4. Use of the vector containing ALDH1A1 the gene and the engineered bacteria in the preparation of a preparation for promoting the proliferation of hair follicle cells, characterized in that: The engineered bacteria include recombinant Escherichia coli.

5. The application of ALDH1A1 protein in the preparation of agents that promote hair follicle cell proliferation, characterized in that: The amino acid sequence of the ALDH1A1 protein is as shown in SEQ ID NO.

4.

6. The application of the ALDH1A1 protein according to claim 5 in the preparation of a hair follicle cell proliferation-promoting agent, characterized in that: The preparation uses the ALDH1A1 protein as the active ingredient.

7. The application of the ALDH1A1 protein according to claim 5 in the preparation of a hair follicle cell proliferation-promoting agent, characterized in that: The preparation includes shampoo and hair care products.

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