Alternative Name(s):

Fibrinogen-clotting enzyme (Snake venom serine protease) (SVSP) (Venombin B)

Species: (Organism)

Agkistrodon contortrix contortrix (Southern copperhead)

Gene Names:

N/A

Tag info:

N-terminal 10xHis-tagged and C-terminal Myc-tagged

Target Protein AA Sequence:

VVGGDECNINEHRFLVAIFNSNGFVCSGTLINQEWVLTAAHCDSTDFQIKLGAHSKKVLNEDEQIRNPKEKFICPNKKNDEVLDKDIMLIKLDSRVSNSEHIAPLSLPSSPPSVGSVCHIMGWGSITPIEVTFPDVPHCAYINLLDDAACQPGYPEVLPEYRTLCAGILEGGKDTCNYDSGGPLICNGQFQGIVSYGAHPCGQSLKPGIYTKVFDYNDWIQSIIAGNTAATCPP

Expression Region:

1-234aa

Subcellular Location:

Secreted

Tissue Specificity:

Expressed by the venom gland.

Protein Length:

Full Length

Pathway:

Mol. Weight:

32.4 kDa

Purity:

Greater than 85% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Others

Function:

Thrombin-like snake venom serine protease that cleaves beta chain of fibrinogen (FGB), releasing fibrinopeptide B. Has a coagulant activity activating blood coagulation factors V (F5) and XIII (F13A1).

Involvement in disease:

Relevance:

Thrombin-like snake venom serine protease that cleaves beta chain of fibrinogen (FGB), releasing fibrinopeptide B. Has a coagulant activity activating blood coagulation factors V (F5) and XIII (F13A1).

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Peptidase S1 family, Snake venom subfamily

Reference:

"A novel venombin B from Agkistrodon contortrix contortrix: evidence for recognition properties in the surface around the primary specificity pocket different from thrombin." Amiconi G., Amoresano A., Boumis G., Brancaccio A., De Cristofaro R., De Pascalis A., Di Girolamo S., Maras B., Scaloni A. Biochemistry 39:10294-10308(2000)