Recombinant Human Keratin, Type I Cytoskeletal 10 (KRT10) Protein (His)

Name: Recombinant Human Keratin, Type I Cytoskeletal 10 (KRT10) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08175P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Keratin, Type I Cytoskeletal 10 (KRT10) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P13645
Target Symbol	KRT10
Synonyms	BCIE; BIE; CK 10; CK-10; Cytokeratin-10; EHK; K10; K1C10_HUMAN; Keratin 10; Keratin 10 type I; Keratin; Keratin type i cytoskeletal 10; Keratin type I cytoskeletal 59 kDa ; Keratin-10; Keratin10; KPP; KRT10; type I cytoskeletal 10
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	EQLAEQNRKDAEAWFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLE
Expression Range	326-443aa
Protein Length	Partial
Mol. Weight	15.7kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays a role in the establishment of the epidermal barrier on plantar skin.; (Microbial infection) Acts as a mediator of S.aureus adherence to desquamated nasal epithelial cells via clfB, and hence may play a role in nasal colonization.; (Microbial infection) Binds S.pneumoniae PsrP, mediating adherence of the bacteria to lung cell lines. Reduction of levels of KRT10 keratin decrease adherence, overexpression increases adherence. Neither protein has to be glycosylated for the interaction to occur.
Subcellular Location	Secreted, extracellular space. Cell surface.
Protein Families	Intermediate filament family
Database References	HGNC: 6413 OMIM: 113800 KEGG: hsa:3858 STRING: 9606.ENSP00000269576 UniGene: Hs.99936
Associated Diseases	Epidermolytic hyperkeratosis (EHK); Ichthyosis annular epidermolytic (AEI); Erythroderma, ichthyosiform, congenital reticular (CRIE)
Tissue Specificity	Seen in all suprabasal cell layers including stratum corneum. Expressed on the surface of lung cell lines.

Gene Functions References

The molecular diagnostics by the whole exome sequencing showed a novel de novo (c.1374-2A>C) mutation in the KRT10 gene responsible for the development of IWC (KRT10 defect was confirmed by immunofluorescent study). Concurrently, the m.14484T>C mutation in mitochondrial MTND6 gene (characteristic for Leber's hereditary optic neuropathy or LHON) was detected in patient, his mother and brother PMID: 28944608
KRT10 gene mutation was present in all of the affected individuals, but absent in the five unaffected and 100 ethnically-matched healthy controls. PMID: 27212473
Mutations in the highly conserved helix initiation motif of K10 were associated with mild or severe form of epidermolytic ichthyosis PMID: 26373619
Report genetic/clinical spectrum of KRT10 mutations in keratinopathic ichthyosis. PMID: 26581228
We present an autosomal dominant pedigree with epidermolytic ichthyosis resulting from a new heterozygous missense mutation in keratin 10. PMID: 26338057
recombinant adenovirus-mediated overexpression of KRT10 and PTEN may improve the cisplatin resistance of ovarian cancer in vitro and in vivo PMID: 26125866
findings provide structural insights into phenotypic variation in epidermolytic ichthyosis due to KRT10 mutations PMID: 26176760
The diagnosis of ichthyosis with confetti was confirmed by the identification of 2 previously unreported mutations in intron 6 and exon 7 of KRT10. PMID: 24626314
We present the spectrum of clinical variability of ichthyosis with confetti in 6 patients with confirmed mutations in KRT10. PMID: 25210931
Case Report: extensive postzygotic mosaicism for a novel keratin 10 mutation in epidermolytic ichthyosis. PMID: 24096702
Data indicate that KRT10 is a downstream molecule of PTEN which improves cisplatin-resistance of ovarian cancer cells. PMID: 24434152
Most of the orthokeratotic dysplasia constituent cells were immunopositive for keratin 10, but not for keratins 13, 17 or 19. PMID: 22734720
Molecular mimicry between HSP 65 of Mycobacterium leprae and cytokeratin 10 of the host keratin play the role in pathogenesis of leprosy. PMID: 23121977
Pneumococcal ligands K10, laminin receptor and platelet-activating factor receptor are elevated in aged lungs and contribute to the enhanced susceptibility to pneumonia. PMID: 21615674
mapping and identifying disease-causing mutations in gene encoding KRT10 in ichthyosis with confetti; high frequency of somatic reversion suggests revertant stem cell clones are under positive selection and/or rate of mitotic recombination is elevated PMID: 20798280
Data show that TIMP-1 and cytokeratin-10 were identified as 2 newly synthesized secreted proteins in PMID: 19904223
Expression was altered in oral lichen planus lesions PMID: 19776502
Mutations in codon 156 of K10, i.e. R156S, R156P, R156H were found in epidermolytic hyperkeratosis. PMID: 12234709
cytokeratin 10 molecules were shown to be exposed on the surface of both desquamated nasal epithelial cells and keratinocytes; Staphylococcus aureus clumping factor B (ClfB) was shown to bind to cytokeratin K10 from the desquamated nasal epithelial cells PMID: 12427098
Impaired NF-kappa B activation and increased production of tumor necrosis factor alpha is observed in transgenic mice expressing keratin K10 in the basal layer of the epidermis. PMID: 12566451
normal cornified cell envelope is formed during the process of human epidermal keratinization, even if the suprabasal keratin filament network is disrupted as with this particular K10 mutation, M150T in BCIE PMID: 14705805
cytokeratin 10 may have a role in progression of head and neck squamous cell carcinoma. PMID: 15254692
We demonstrate that a recessive mutation in KRT10 leading to a complete human K10 knockout can cause EHK PMID: 16505000
Candidate autoantigen in chronic, antibiotic-resistant Lyme arthritis. PMID: 16888010
Squamous cell carcinoma (SCC) in mature cystic teratoma (MCT) expressed CK10 less frequently, but CK18 more frequently. SCC in MCT may be derived from metaplastic squamous epithelium. PMID: 17542994
Mild recessive bullous congenital ichthyosiform erythroderma due to a previously unidentified homozygous keratin 10 nonsense mutation. PMID: 18219278
siRNA for PRKD1 resulted in reduction of mRNA levels of PKD1, altered cell phenotype and promotion of keratinocyte differentiation, demonstrated by increased expression of involucrin and K10 mRNAs PMID: 18259765
CK10 alone, or in combination with CK19, can be a novel predictor for poor prognosis of hepatocellular carcinoma patients after curative resection. PMID: 18559605
EHK is an autosomal dominant disorder of keratinization, caused by mutations in either the KRT1 or KRT10 genes. Our patient presents EHK with palmoplantar involvement and KRT10 mutation. PMID: 19443303
premature termination codon of KRT10 maybe involved in recessive epidermolytic hyperkeratosis PMID: 19474805
Infection by HPV may alter the differentiation status of the epidermis, leading to delayed or absent expression of cytokeratin 10. PMID: 19515043

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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