Human WAP, kazal, immunoglobulin, kunitz and NTR domain-containing protein 2 (WFIKKN2) Protein

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Description
Human WFIKKN2 Protein is a recombinant protein from Human produced in HEK293 Cells. A DNA sequence encoding the human WFIKKN2 (NP_783165.1) extracellular domain (Met 1-His 576) was expressed, with a polyhistidine tag at the C-terminus.
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Product specifications
Category | Proteins and Peptides |
Immunogen Target | WFIKKN2 |
Host | HEK293 cells |
Origin | Human |
Observed MW | Molecular Weight: 61.4 kDa Sequence Fragment: Met1-His576 Tag: C-terminal His tag Validity: The validity for this protein is 12 months. |
Expression | Recombinant |
Purity | > 96% (SDS-PAGE) |
Size 1 | 50 µg |
Form | |
Tested Applications | SDS-PAGE |
Buffer | Lyophilized from sterile PBS, pH 7.4. |
Availability | Shipped within 5-15 working days. |
Storage | Aliquot and store at -20°C or -80°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
NCBI Accession | NP_783165.1 |
Alias | GASP-1,WFDC20B,hGASP-1,WFIKKNRP,WFIKKN-related protein,Growth and differentiation factor-associated serum protein 1,GASP-1,hGASP-1 |
Background | Protein WFIKKN2 |
Status | RUO |
Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
WAP follistatin/kazal immunoglobulin kunitz and netrin domain containing 2 (WFIKKN2) shares structural and functional similarities with WFIKKN1, including its role as a protease inhibitor and regulator of extracellular matrix dynamics. It is particularly known for its interaction with growth differentiation factors such as GDF8 (myostatin) and GDF11, inhibiting their activity and contributing to the regulation of muscle and skeletal growth. WFIKKN2 is expressed in various tissues, including the liver, kidney, and skeletal muscle, and plays a crucial role in maintaining tissue homeostasis by modulating protease activity during processes like inflammation, repair, and cellular migration. In cancer biology, WFIKKN2 has been implicated in controlling tumor progression and metastasis by influencing proteolytic activity in the tumor microenvironment. Additionally, WFIKKN2 has potential therapeutic applications in metabolic and degenerative disorders due to its regulatory effects on signaling pathways associated with growth differentiation factors. The interplay between WFIKKN2 and other extracellular molecules continues to be a focus of study, with particular interest in its potential to serve as a biomarker or therapeutic target in diseases characterized by abnormal proteolysis or tissue remodeling.
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