Recombinant Human Keratin, Type I Cytoskeletal 14 (KRT14) Protein (His-SUMO)

Name: Recombinant Human Keratin, Type I Cytoskeletal 14 (KRT14) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10739P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Keratin, Type I Cytoskeletal 14 (KRT14) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P02533
Target Symbol	KRT14
Synonyms	CK 14; CK-14; ck14; Cytokeratin 14; Cytokeratin-14; Cytokeratin14; Dowling Meara; EBS3; EBS4; Epidermolysis bullosa simplex; K14; K1C14_HUMAN; Keratin 14 (epidermolysis bullosa simplex, Dowling-Meara, Koebner); Keratin 14; Keratin; Keratin type I cytoskeletal 14; Keratin, type I cytoskeletal 14; Keratin-14; Keratin14; Koebner; Krt 14; Krt14; NFJ; OTTHUMP00000164624; type I cytoskeletal 14
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MTTCSRQFTSSSSMKGSCGIGGGIGGGSSRISSVLAGGSCRAPSTYGGGLSVSSSRFSSGGACGLGGGYGGGFSSSSSSFGSGFGGGYGGGLGAGLGGGFGGGFAGGDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLSSSQFSSGSQSSRDVTSSSRQIRTKVMDVHDGKVVSTHEQVLRTKN
Expression Range	1-472aa
Protein Length	Full Length
Mol. Weight	67.6kDa
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	The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.
Subcellular Location	Cytoplasm. Nucleus. Note=Expressed in both as a filamentous pattern.
Protein Families	Intermediate filament family
Database References	HGNC: 6416 OMIM: 125595 KEGG: hsa:3861 STRING: 9606.ENSP00000167586 UniGene: Hs.654380
Associated Diseases	Epidermolysis bullosa simplex, Dowling-Meara type (DM-EBS); Epidermolysis bullosa simplex, Weber-Cockayne type (WC-EBS); Epidermolysis bullosa simplex, Koebner type (K-EBS); Epidermolysis bullosa simplex, autosomal recessive 1 (EBSB1); Naegeli-Franceschetti-Jadassohn syndrome (NFJS); Dermatopathia pigmentosa reticularis (DPR)
Tissue Specificity	Expressed in the corneal epithelium (at protein level). Detected in the basal layer, lowered within the more apically located layers specifically in the stratum spinosum, stratum granulosum but is not detected in stratum corneum. Strongly expressed in the

Gene Functions References

High CK14 expression is associated with lymph node metastasis in oral squamous cell carcinoma. PMID: 30066921
Efficient homology-directed repair of a dominant negative KRT14 mutation via CRISPR/Cas9 nickases in epidermolysis bullosa simplex patients' keratinocytes has been reported. PMID: 28888469
Immunocytochemical staining using cocktail antibody targeting p63/CK14 was useful for the differential diagnosis of FA and DCIS in FNAC of the breast. PMID: 28685877
the findings show that squamous and micropapillary bladder cancers have different expression patterns of CK14 and FOXA1 and suggest that they arise from distinct precursors. PMID: 28721490
PADI4 contributes to gastric tumorigenesis by upregulating CXCR2, KRT14 and TNF-alpha expression. PMID: 27556695
The novel c.1234A>G(p.Ile412Val) mutation of the KRT14 gene is probably responsible for the disease. PMID: 28777847
Keratin14/p63-positive epithelial proliferations suggest benign breast disease. PMID: 28630050
K14 was coexpressed with alphav-integrin in fetal and adult corneas and cultured corneolimbal epithelium, and colony-forming efficiency (an indicator of stem cell activity) was similar in cells from both sources. PMID: 26956898
Loss of keratin 14 is associated with epidermolysis bullosa. PMID: 27798626
contributes to collective invasion of salivary adenoid cystic carcinoma and may be a biomarker of worse prognosis PMID: 28152077
vimentin regulates the differentiation switch via modulation of K5/K14 expression. Moreover, because there was a significant correlation between high vimentin-K14 expression and recurrence/poor survival in oral cancer patients, vimentin-K14 together may prove to be the novel markers for the prognostication of human oral cancer. PMID: 28225793
We concluded that smoking habits were capable of inducing changes in global DNA methylation, miR-9-3 methylation status and K19 expression. PMID: 27543926
data demonstrates that keratinocyte migration requires the interaction between vimentin and keratins at the -YRKLLEGEE- sequence at the helical 2B domain of viment PMID: 27072292
findings reveal K14 as a key regulator of metastasis and establish the concept that K14(+) epithelial tumor cell clusters disseminate collectively to colonize distant organs PMID: 26831077
all keratins tested, except for keratin 14, were evenly expressed in all trophoblast cells. Keratin 14 was expressed in a subset of CK7 positive cells PMID: 26430881
report a family with a novel heterozygous missense mutation p.Leu418Gln in the KRT14 gene causing epidermolysis bullosa simplex with variable phenotype PMID: 24981776
investigated a family in which 1 of 3 children was diagnosed with a localized form of epidermolysis bullosa simplex and there was no family history of blistering; results argue against parental somatic and germline mosaicism in the family and suggest the novel p.Val270Ala mutation in KRT14 also represents a de novo event which occurred in the proband PMID: 23774754
KRT14 protein genetic mutation is a good indicator of disease progression in patient diagnosed with epidermolysis bullosa simplex. PMID: 25961909
Analysis of K14 variants with single or multiple substitutions of cysteine residues points to a spatial and temporal hierarchy in how Cys-4/Cys-40 and Cys-367 regulate keratin assembly in vitro and filament dynamics in live keratinocytes PMID: 26216883
BerEp4 alone is unreliable for differentiation between BCCm (basal cell carcinoma with squamous metaplasia) and bSCC (basaloid squamous cell carcinoma). The addition of either CK14 or CK17 will augment BCCm versus bSCC differential diagnosis. PMID: 24168496
hypothesize a positive feedback model in which mutant (R125P) K14 triggers JNK signalling, leading to increased AP1-dependent expression of K14, which in turn amplifies JNK signalling further PMID: 23528216
p53 acts as a co-repressor to down-regulate K14 expression by binding to SP1. PMID: 22911849
p53 acts as a co-repressor to down-regulate K14 expression by binding to SP1 during epidermal cell differentiation. PMID: 22911849
One isoform of p63, TAp63alpha, can activate an epidermal basal cell marker, keratin 14. PMID: 22577164
Mutant K14-R125P filaments and/or networks in human keratinocytes are mechanically defective in their response to large-scale deformations. PMID: 22363617
This study adds two more novel recessive mutations in this gene associated with epidermolysis bullosa simplex. This is the first occurence in a Mediterranean population. PMID: 21623745
Fascin and CK14 are highly expressed in squamous cell carcinoma, compared with other histological types of carcinoma. PMID: 21223690
keratin 14 functional knockout causes severe recessive epidermolysis bullosa simplex, and questions the haploinsufficiency model of Naegeli-Franceschetti-Jadassohn syndrome PMID: 21734713
Mutation analysis of an epidermolysis bullosa simplex family revealed that affected individuals were heterozygous for a, to our knowledge, previously unreported mutation of c.1237G>C (p.Ala413Pro) in KRT14. PMID: 21593775
heterozygous G to A transition was found at nucleotide postion 1231 in exon 6 of KRT14 in family with epidermolysis bullosa simplex, generalized PMID: 21413954
autoantibodies in Scurfy mice and patients with IPEX target keratin 14 PMID: 20147963
analysis of a keratin 14 hotspot mutation in the Dowling-Meara type of epidermolysis bullosa simplex PMID: 19854623
new heterozygous amino acid substitution polymorphism in the variable keratin 14 N-terminal head domain (KRT14:c.88C>T, p.Arg30Cys) PMID: 19797037
A spontaneous CD8 T cell-dependent autoimmune disease to an antigen expressed under the human keratin 14 promoter. PMID: 12165543
Three novel KRT14 mutations identified in 9 Epidermolysis bullosa simplex patients. PMID: 12655565
investigated novel KRT14 missense mutations in epidermolysis bullosa simplex in a cellular expression system in order to analyse their effects on the keratin cytoskeleton PMID: 12930305
Keratin 14 has a role in binding to TNFalpha receptor-associated death domain (TRADD), and in susceptibility of keratinocytes to caspase-8-mediated apoptosis PMID: 14660619
novel recessive missense mutation in epidermolysis bullosa simplex PMID: 15654986
Novel mutations within KRT14 are associated with epidermolysis bullosa simplex. PMID: 16786515
Heterozygous nonsense or frameshift mutations in KRT14 were found to segregate with Naegeli-Franceschetti-Jadassohn syndrome or dermatopathia pigmentosa reticularis trait in five families. PMID: 16960809
These studies provide a potential mechanism by which deltaNp63 directly governs the expression of K14 in a keratinocyte-specific manner. PMID: 17159913
study presents a missense mutation in exon 1 of K14, R125C, identified in the affected individuals of a Chinese family with epidermolysis bullosa simplex-Dowling-Meara (EBS-DM) PMID: 17659012
Better basal gene expression was observed by co-cultured respiratory epithelial cells compared to dispase dissociated cells. PMID: 17891046
K14 and K16 were detected in the tumour cells, suggesting differentiation towards the outer root sheath beneath the orifice of the sebaceous duct. PMID: 18005116
Naegeli-Franceschetti-Jadassohn syndrome results from haploinsufficiency for K14 and increased susceptibility of keratinocytes to pro-apoptotic signals may be involved in the pathogenesis of this ectodermal dysplasia syndrome PMID: 18049449
Transgenic mice were generated using the keratin-14 promoter/enhancer to direct expression of wild-type human CXCR2 (K14hCXCR2 WT) or mutant CXCR2. PMID: 18505935
expression of human K14 initiates squamous differentiation program in the mouse lung, but fails to promote squamous maturation PMID: 18701433
Including the present case, 8 of the 13 families have the R125C or R125H mutation; eight have mutations in KRT14, and five have mutations in KRT5 PMID: 18717745
Cataracts in transgenic mice caused by a human papillomavirus type 18 E7 oncogene driven by KRT1-14 are reported. PMID: 18723014
Infection by HPV may alter the differentiation status of the epidermis, leading to a major expression of cytokeratin 14 PMID: 19515043

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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.

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