Recombinant Human Vitronectin/VTN (C-6His) #abs04331

abs04331-10ug

1-2 Weeks

46

abs04331-50ug

1-2 Weeks

123

abs04331-500ug

1-2 Weeks

642

abs04331-1mg

1-2 Weeks

873

Description

Our Mammalian expression system is responsible for producing Recombinant Human Vitronectin. The target gene, which encodes Asp20-Leu478, is expressed with a 6His tag at the C-terminus.

Other names

VN, Serum-Spreading Factor, S-Protein, Vitronectin, VTN, V75 - these are all different names for a protein that plays an important role in the human body. Vitronectin is a glycoprotein that is found in blood plasma and extracellular matrix. It helps with cell adhesion, spreading, and migration, and is also involved in blood clotting and immune response.
VN has been studied extensively for its potential therapeutic applications in a variety of medical conditions such as cancer, cardiovascular disease, and autoimmune disorders. Furthermore, serum concentrations of VN have been linked to various diseases, including liver disease, diabetes, and arthritis.
S-Protein, another commonly used name for VN, refers to its function as a regulator of the protease activity that is necessary for wound healing and tissue repair. In addition, VTN works as a chaperone protein, facilitating the correct folding and transport of other proteins in the body.
V75, which is the truncated form of VN, has been found to be important in the regulation of bone metabolism and the prevention of osteoporosis. Understanding the functions and roles of Vitronectin and its various forms can provide insights into disease mechanisms and the development of effective therapies.

Source

Human Cells

Format

pH 8.0 lyophilized from a 0.2 μm filtered solution of 20mM TrisHCl, 150mM NaCl. Let's rearrange the content to maintain the original information: The solution containing 20mM TrisHCl and 150mM NaCl with a pH of 8.0 was filtered through a 0.2 μm filter before being lyophilized.

Properties

aa_sequence

EFCSQYDKPKGQVGGDTTGQTLAVALADAGQSGEKTTETSYKRAEKHTDDGYQVCGVDVETEDPTQ NGDVTQGPPPEYVYYPDETDPNCDDEEGSKDCVCKPMRPATNKEDCSEVKQYTPLLGTVAHSNEEA RETPQGSCGAGDSEDVKQTDPRHHPALELAEPLAEKEVKGPRGQAINTDLAAASYGKSGYGQVLW FYDAPNWALLNFCAGPRQTVMPWGRRELKYAVVFIPQTISALQDNYFAVDTCQEPSYKEDGRVIE MOSYTWGLEKPQRGKERRETKQGRPQRRNWGRSSQNGYLKKHAGLSGGFDRKGPKGEGWVARCYGI SRAFEDRFGDWMPNGPLGGREVLCRGQSTDWTVIPDCAHGYAQQEFRQKGQSEQSDCQECMQKMGQ CCQSYCLFSRFLPKFKYTGWRDYDSPNFRIAKYAWLPNESAAFQMQYFDGSKPYMDCWNNRVAVN ISPYFDGKPDVHGPDKDHGPGHSVCSYQAILAICSRGPNVKSDKGSRSYPDRCQQGDPLHMPAEEG LKFAFRCVREKEDFIRRRLGPNSDVGKRCQRNYTSDAQHSGTSGWKFQVQHLNAIYPGTEWLLSPY NQTVDSIRGFSFMLRDLFLERAWKGPQHPSWKATSCEQEGFSFFDHSAHFELKYAVGKNTTGASSE EPASSERGPGENDYPWPYARANTEMHYLMVNVEDNMSYEGYPLTVMPWVVGMLTQVWMIDEDGRR CRGPNTASCII Please generate a highly similar content by rearranging the above content, ensuring that the generated content is based on the original text information.

Concentration

Based on the results of reducing SDS-PAGE, the purity of the sample is found to be greater than 95%. To rephrase this, the sample shows a purity level of over 95% when analyzed via SDS-PAGE gel electrophoresis.

Endotoxin_level

The LAL test determines that the content is below 0.1 ng/μg (1 IEU/μg).

Reconstitution

Before opening, always centrifuge the tubes. Avoid mixing by vortex or pipetting. It is advisable not to reconstitute to a concentration lower than 100 μg/ml. Dissolve the protein that has been lyophilized in ddH2O. To avoid damage, divide the reconstituted solution into smaller portions. Be cautious of freeze-thaw cycles.

Target

Background

Human Vitronectin/VTN is a cell adhesion and spreading factor. It can be found in the blood and the extracellular matrix (ECM). Vitronectin interacts with glycosaminoglycans and proteoglycans. The multimeric Vitronectin can efficiently bind to and incorporate into the ECM; Vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Vitronectin can be recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecular. It can as a inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Vitronectin contains an endogenous cleavage site, plus cleavage sites for elastase, thrombin, and plasmin.

Accession

P04004