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  • Cytokines
  • Growth factors
  • Chemokines
  • Cd antigens
  • Neurotrophins
  • Hormones
  • Enzymes
  • Viral antigens
  • Recombinant proteins
  • Natural proteins
  • Monoclonal antibodies
  • Polyclonal antibodies
  • Thermal Packaging
  • Tumor Necrosis Factor

    Tumor Necrosis Factor

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  • 4-1BB

    4-1BB

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  • Adiponectin

    Adiponectin

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  • AIF1

    AIF1

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  • Other Cytokines

    Other Cytokines

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  • AITRL

    AITRL

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  • Angiopoietin

    Angiopoietin

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  • Apolipoprotein

    Apolipoprotein

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  • B-Cell Activating Factor

    B-Cell Activating Factor

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  • Beta Defensin

    Beta Defensin

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  • Bone Morphogenetic Protein

    Bone Morphogenetic Protein

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  • B type Natriuretic Peptide

    B type Natriuretic Peptide

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  • BST

    BST

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  • Betacellulin

    Betacellulin

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  • Cardiotrophin

    Cardiotrophin

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  • Activin

    Activin

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  • Fibroblast Growth Factor

    Fibroblast Growth Factor

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  • Other Growth Factors

    Other Growth Factors

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  • CSF

    CSF

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  • CTGF

    CTGF

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  • IGFBP

    IGFBP

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  • VEGF Protein

    VEGF Protein

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  • EGF

    EGF

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  • Epigen

    Epigen

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  • Erythropoietin

    Erythropoietin

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  • Insulin-Like Growth Factor

    Insulin-Like Growth Factor

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  • Growth Hormone

    Growth Hormone

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  • HDGF

    HDGF

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  • Hepatocyte Growth Factor

    Hepatocyte Growth Factor

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  • Insulin

    Insulin

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  • BCA-1/ BLC (CXCL13)

    BCA-1/ BLC (CXCL13)

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  • BRAK (CXCL14)

    BRAK (CXCL14)

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  • C-10 (CCL6)

    C-10 (CCL6)

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  • Other Chemokines

    Other Chemokines

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  • MEC (CCL28)

    MEC (CCL28)

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  • LD78-beta (CCL3L1)

    LD78-beta (CCL3L1)

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  • CTACK (CCL27)

    CTACK (CCL27)

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  • CXCL16

    CXCL16

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  • CXCL17

    CXCL17

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  • Platelet Factor-4 (CXCL4)

    Platelet Factor-4 (CXCL4)

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  • ENA-78 (CXCL5)

    ENA-78 (CXCL5)

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  • Eotaxin (CCL11,24,26)

    Eotaxin (CCL11,24,26)

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  • Exodus-2 (CCL21)

    Exodus-2 (CCL21)

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  • Fractalkine (CX3CL1)

    Fractalkine (CX3CL1)

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  • CXCL6

    CXCL6

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  • Other CD Antigens

    Other CD Antigens

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  • CD14

    CD14

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  • CD164

    CD164

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  • CD1

    CD1

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  • CD2

    CD2

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  • CD200

    CD200

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  • CD207

    CD207

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  • CD226

    CD226

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  • CD23

    CD23

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  • CD244

    CD244

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  • CD247

    CD247

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  • CD27

    CD27

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  • CD274

    CD274

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    CD300

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  • CD33

    CD33

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  • Other Neurotrophins

    Other Neurotrophins

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  • Beta-NGF

    Beta-NGF

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  • BDNF

    BDNF

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  • CDNF

    CDNF

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  • CNTF

    CNTF

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  • GDNF

    GDNF

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  • Glia Maturation Factor

    Glia Maturation Factor

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  • MANF

    MANF

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  • Midkine

    Midkine

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  • Neuroglobin

    Neuroglobin

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  • Neurotrophic factors

    Neurotrophic factors

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  • Neuregulin

    Neuregulin

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  • Neuropilin

    Neuropilin

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  • Pigment Epithelium-Derived Factor

    Pigment Epithelium-Derived Factor

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  • Pleiotrophin

    Pleiotrophin

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  • Peptide Hormones

    Peptide Hormones

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  • Other Hormones

    Other Hormones

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  • HCG

    HCG

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  • Endothelin

    Endothelin

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  • Exendin

    Exendin

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  • FSH

    FSH

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  • Glucagon

    Glucagon

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  • GHRP

    GHRP

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  • GLP

    GLP

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  • Thyrostimulin

    Thyrostimulin

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  • Inhibin A

    Inhibin A

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  • LHRH

    LHRH

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  • Melanotan

    Melanotan

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  • Procalcitonin

    Procalcitonin

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  • PTH

    PTH

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  • Peroxiredoxin

    Peroxiredoxin

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  • Peptidase

    Peptidase

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  • Synthetase

    Synthetase

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  • Transferase

    Transferase

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  • Hydrolase

    Hydrolase

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  • Dehydrogenase

    Dehydrogenase

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  • ACE2

    ACE2

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  • Esterase

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  • Protein Kinases

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  • Other Enzymes

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  • Phosphatase

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  • Deaminase

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  • Oxygenase

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  • Adenylate Kinase

    Adenylate Kinase

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  • Lyase

    Lyase

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  • Chagas

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  • Feline Leukemia Virus

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  • Hepatitis A

    Hepatitis A

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  • Other

    Other

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  • Actin

    Actin

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  • ADAM

    ADAM

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  • Complement Component

    Complement Component

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  • Ag85

    Ag85

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  • Eukaryotic Translation Initiation Factor

    Eukaryotic Translation Initiation Factor

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  • Anterior Gradient Protein

    Anterior Gradient Protein

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  • Heat Shock Protein

    Heat Shock Protein

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  • Alpha-2-HS-Glycoprotein

    Alpha-2-HS-Glycoprotein

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  • Hemoglobin

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  • Allergy

    Allergy

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  • Anaplasma

    Anaplasma

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  • Angiogenin

    Angiogenin

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  • Ankyrin Repeat Domain

    Ankyrin Repeat Domain

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  • Annexin

    Annexin

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  • Other Natural Proteins

    Other Natural Proteins

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  • Aprotinin

    Aprotinin

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  • Transferrin

    Transferrin

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  • Avidin

    Avidin

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  • Anti Coagulation Factors

    Anti Coagulation Factors

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  • Natural Albumin

    Natural Albumin

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  • Natural Coagulation Factors

    Natural Coagulation Factors

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  • Fibronectin

    Fibronectin

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  • Thrombin

    Thrombin

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  • Anti Human Enzyme

    Anti Human Enzyme

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  • Other Monoclonal Antibodies

    Other Monoclonal Antibodies

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  • Anti Human Cytokine

    Anti Human Cytokine

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  • Anti Human Heat Shock Protein

    Anti Human Heat Shock Protein

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  • Anti Mouse Lymphocyte

    Anti Mouse Lymphocyte

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  • Anti Human Chemokine

    Anti Human Chemokine

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  • Anti Human Lymphocyte

    Anti Human Lymphocyte

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  • Anti Viral Monoclonal

    Anti Viral Monoclonal

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  • Anti Mouse Cytokine

    Anti Mouse Cytokine

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  • Anti-GST Monoclonal

    Anti-GST Monoclonal

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  • Other Polyclonal Antibodies

    Other Polyclonal Antibodies

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  • Anti Viral

    Anti Viral

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  • Anti-GST Monoclonal

    Anti-GST Monoclonal

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Search results

1000 results found for “Chromogranin”

Name

Description

Product #

Price

Quantity

Shipping Method

  • View Data Sheet

    Name :

    Thrombin

    Description:

    Human Thrombin

    Product # :

    PRO-339

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • biological activity
    • More Info

    Description

    Thrombin was purified from human plasma.

    Source

    Human Plasma.

    Formulation

    Lyophilized protein containing mannitol, sodium chloride, calcium chloride.

    Biological Activity

    The specific activity was found to be 116 US Units/mg protein.

    More Info

    • Introduction

      Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

    • Physical Appearance

      lyophilized powder.

    • Stability

      Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized human thrombin in sterile a 0.9% NaCl solution at 500U/ml.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Thrombin Human
  • View Data Sheet

    Name :

    KRT18 Human

    Description:

    Cytokeratin 18 Human Recombinant

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    PRO-349

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
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    • More Info

    Description

    Cytokeratin 18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a calculated molecular mass of 48,201 Dalton, showing a 45kDa band on SDS-page, pI-5.7.The KRT18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CK-18 although stable at room temperature for 3 weeks, should be stored between 2-8°C. Upon reconstitution CK-18 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized 1mg CK-18 in sterile 18MΩ-cm H2O not less than 700µl, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

      Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Krt18 Human
  • View Data Sheet

    Name :

    Fibronectin Recombinant

    Description:

    Fibronectin Human Recombinant

    Product # :

    PRO-2621

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Fibronectin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 574 amino acids and having a molecular mass of 62.6kDa. The Fibronectin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, with 5 % Trehalose and 0.02 % Tween-20.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Was measured by its ability to support cell attachment and spreading when used as a substratum for cell culture. The recommended concentration in this application for this effect is typically 1-5 μg/cm2. Fibronectin can also be added to the media to support cell spreading at a concentration of 0.5-50 μg/ml. Optimal concentrations will need to be determined for individual user applications.

    More Info

    • Introduction

      Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Fibronectin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Fibronectin Recombinant
  • View Data Sheet

    Name :

    Streptavidin-NC

    Description:

    Streptavidin-NC Recombinant

    Product # :

    PRO-338

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Recombinant Streptavidin-NC produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 24kDa. Streptavidin-NC is engineered to bind to nitrocellulose.

    Source

    Escherichia Coli.

    Formulation

    The sterile solution contains 10mM K2HPO4-KH2PO4, pH 7.3.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Liquid formulation.

    • Stability

      Streptavidin-NC although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Streptavidin Nc
  • View Data Sheet

    Name :

    HCG-b core antibody

    Description:

    Human Chorionic Gonadotropin beta core, Mouse antibody

    Chorionic gonadotropin beta polypeptide, CGB3, hCGB,Choriogonadotropin subunit beta, CG-beta, Chorionic gonadotrophin chain beta.

    Product # :

    ANT-147

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • formulation
    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

    More Info

    • Introduction

      Human chorionic gonadotropin (hCG) is a peptide hormoneproduced in pregnancy, that is made by the embryosoon after conceptionand later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesteroneproduction that is critical for a pregnancyin humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testinggenerally is based on the detection or measurement of hCG.

    • Synonyms

      Chorionic gonadotropin beta polypeptide, CGB3, hCGB,Choriogonadotropin subunit beta, CG-beta, Chorionic gonadotrophin chain beta.

    • Solubility

      Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      purified hCG beta core.

    • Ig Subclass

      mouse IgG2b.

    • Clone

      NYRhCG.

    • Note

      Minimal cross-reactivity with human Luteinizing Hormone b-Core fragment.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Antibody Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Ion exchange column.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cg B Core Antibody
  • View Data Sheet

    Name :

    ProMatrilysin

    Description:

    ProMatrix Metalloproteinase-7 Recombinant

    Product # :

    ENZ-272

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
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    Description

    Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

    Source

    Escherichia Coli.

    Formulation

    The protein contains the following additives 25mM Tris-HCl (pH 7.5),150mM NaCl, 5mM CaCl2, 0.01% Brij-35 and 0.02% NaN3.

    Purity

    Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 1400 IU/mg.

    More Info

    • Physical Appearance

      Sterile clear liquid solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Unit Definition

      One unit is defined as the digestion of 1 µg Azocoll/min at 37°C.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Promatrilysin
  • View Data Sheet

    Name :

    CRP Canine

    Description:

    C-Reactive Protein Canine Recombinant

    C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

    Product # :

    PRO-2663

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    Description

    CRP Canine Recombinant is a single, glycosylated polypeptide chain containing 204 amino acids and having a molecular mass of 23.2kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    CRP filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl and 1mM CaCl2, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.

    • Synonyms

      C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      QIDLDEKAFV FPRESENSYV ILFPQLQKPM KAFTVCLQVY TDLTRPHSLF SYATKSQSNE ILLFKERPGL FSVSVGGSDA FINFPQKFYA PQHFCVTWES VTGLTELWVD GKPMVRASLR RGYTVGSGAS IVLGQEQDSF GGGFDKNQSL VGDIEDVNMW DFVLSPSQIL TLYTTRALSP NVLNWRNLRY ETRGEVFLKK ELWS

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    CRP Canine
  • View Data Sheet

    Name :

    CTF2P Mouse

    Description:

    Neuropoietin Mouse Recombinant

    Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

    Product # :

    CYT-1128

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    • source
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    Description

    Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

    More Info

    • Introduction

      CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.

    • Synonyms

      Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

    • Background

      What is the molecular weight/Mw of CTF2P Protein?
      CTF2P Protein has a total Mw of 19.7kDa.

      What is the source or expression system of CTF2P Protein?
      Escherichia Coli.

      What is the Purity of CTF2P Protein?
      CTF2P Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF2P Protein?
      The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

      What is the amino acid sequence of CTF2P Protein?
      APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

      What applications can CTF2P Protein be used in?
      CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF2P Protein?
      The endotoxin level is minimal, CTF2P Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Neuropoietin Mouse
  • View Data Sheet

    Name :

    Leptin Mouse (D23L)

    Description:

    Leptin D23L Mutant Mouse Recombinant

    Product # :

    CYT-1249

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    • source
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    Description

    Leptin Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin having a molecular mass of 16 kDa and was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Mouse is able to induce proliferation of BA/F3 cells stably transfected with the long form of human leptin receptor but its affinity toward this receptor was ~ 25-fold higher compared to non-mutated mouse leptin.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization Mouse Leptin can be stored at 4°C for 2-3 months. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Mouse in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids is Ala-Val-Pro-Ile-Gln

    • Background

      Leptin’s main part is to regulate long-term energy balance. Leptin produced mainly by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of different cells in the human body. The leptin receptor is found on various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value was calculated by DNA man program.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Leptin Mouse Mutant
  • View Data Sheet

    Name :

    Hepatocyte Growth Factor Human, HEK

    Description:

    Hepatocyte Growth Factor Human Recombinant, HEK

    Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.

    Product # :

    CYT-090

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    Description

    HGF Human Recombinant produced in HEK cells is a glycosylated disulfide-linked heterodimer, containing 697 a.a. (Gln-32 to Ser-728) having a total molecular weight of 80kDa. The HGF is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The HGF was lyophilized from a solution (1mg/ml) containing 10mM Sodium phosphate, 150mM NaCl, 0.01% Tween 80 and 100mM L-Arginine, pH 6.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC50 for this effect is typically 20-40ng/ml.

    More Info

    • Introduction

      Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

    • Synonyms

      Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized HGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Hepatocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728

    • Background

      What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein has a total Mw of 80kDa.

      What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
      HEK.
      What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
      The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC50 for this effect is typically 20-40ng/ml.
      What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
      32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728

      What applications can HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein be used in?
      HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
      The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Hgf Human Hek
  • View Data Sheet

    Name :

    Myostatin Human, His

    Description:

    Myostatin Human Recombinant, His Tag

    GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.

    Product # :

    CYT-445

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    Description

    Total 152AA. M.W. 16.7kDa (calculated). N-terminal His-tag and spacer (43AA – highlighted). The AA sequence of the human myostatin part of the fusion protein is corresponding to the UniProtKB/Swiss-Prot entry O14793.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M acetate buffer, pH 4.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myostatin (GDF-8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ? superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.

    • Synonyms

      GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.

    • Physical Appearance

      Filtered white lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDPSSRSAVR SRRDFGLDCD EHSTESRCCR YPLTVDFEAFGWDWIIAPKR YKANYCSGEC EFVFLQKYPH THLVHQANPR GSAGPCCTPT KMSPINMLYF NGKEQIIYGKIPAMVVDRCG CS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Myostatin Human Fc
  • View Data Sheet

    Name :

    CDKN1A Human (20-149)

    Description:

    Cyclin-Dependent Kinase Inhibitor 1A (20-149 a.a.) Human Recombinant

    Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

    Product # :

    PKA-137

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    Description

    The CDKN1A Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CDKN1A His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 130 amino acid residues of the CDKN1A Human, 20-149 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized CDKN1A at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLEGDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLVPRSGEQAEGS PGGPGDSQGR KRRQTSMTDF

    • Background

      CDKN1A gene in humans plays an important role in maintaining genomic stability which is critical to cancer prevention and proper function of regular cellular processes. CDKN1A plays a main role in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. CDKN1A, along with CDK2 complexes aids to prevent kinase activity and inhibits progression through G1/S. CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cdkn1A Protein
  • View Data Sheet

    Name :

    RGS16 Human

    Description:

    Regulator of G-Protein Signaling 16 Human Recombinant

    A28-RGS14, A28-RGS14P, RGS-R, Regulator of G-protein signaling 16, RGS16, Retinally abundant regulator of G-protein signaling, Retinal-specific RGS, hRGS-r, RGSR.

    Product # :

    PRO-798

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    Description

    RGS16 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (1-202 a.a.) and having a molecular mass of 24.9 kDa. The RGS16 is fused to a 20 amino acid His Tag at N-terminal and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RGS16 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4), 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RGS16 is part of the ''regulator of G protein signaling'' family. RGS16 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. RGS16 Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha. RGS16 regulates the kinetics of signaling in the phototransduction cascade.

    • Synonyms

      A28-RGS14, A28-RGS14P, RGS-R, Regulator of G-protein signaling 16, RGS16, Retinally abundant regulator of G-protein signaling, Retinal-specific RGS, hRGS-r, RGSR.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MCRTLAAFPT TCLERAKEFK TRLGIFLHKS ELGCDTGSTG KFEWGSKHSK ENRNFSEDVL GWRESFDLLL SSKNGVAAFH AFLKTEFSEE NLEFWLACEE FKKIRSATKL ASRAHQIFEE FICSEAPKEV NIDHETRELT RMNLQTATAT CFDAAQGKTR TLMEKDSYPR FLKSPAYRDL AAQASAASAT LSSCSLDEPS HT.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Rgs16 Human
  • View Data Sheet

    Name :

    Streptavidin

    Description:

    Streptavidin Recombinant

    Product # :

    PRO-791

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    • More Info

    Description

    Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized in 10mM potassium phosphate buffer pH 6.5.

    Purity

    Greater than 98.0% as determined by SDS-PAGE and HPLC.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.

    • Solubility

      It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
      GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
      EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS.

    • Proteolytic Activity

      < 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).

    • Specific Activity

      > 17U/mg (one unit binds 1 μg D-biotin).

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Streptavidin Recombinant
  • View Data Sheet

    Name :

    CTSD Mouse

    Description:

    Cathepsin-D Mouse Recombinant

    Ctsd, CatD, CD, Cathepsin D.

    Product # :

    ENZ-1017

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    Description

    CTSD produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-410 a.a.) and having a molecular mass of 44.0kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTSD is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTSD protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.

    More Info

    • Introduction

      Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.

    • Synonyms

      Ctsd, CatD, CD, Cathepsin D.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      IIRIPLRKFT SIRRTMTEVG GSVEDLILKG PITKYSMQSS PKTTEPVSEL LKNYLDAQYY GDIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KILDIACWVH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSDQSKARGI KVEKQIFGEA TKQPGIVFVA AKFDGILGMG YPHISVNNVL PVFDNLMQQK LVDKNIFSFY LNRDPEGQPG GELMLGGTDS KYYHGELSYL NVTRKAYWQV HMDQLEVGNE LTLCKGGCEA IVDTGTSLLV GPVEEVKELQ KAIGAVPLIQ GEYMIPCEKV SSLPTVYLKL GGKNYELHPD KYILKVSQGG KTICLSGFMG MDIPPPSGPL WILGDVFIGS YYTVFDRDNN RVGFANAVVL LEHHHHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ctsd Mouse
  • View Data Sheet

    Name :

    GH Chicken

    Description:

    GH Chicken Recombinant

    GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH 1, 

    Product # :

    CYT-430

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    Description

    GH Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids with an additional Ala at its N-terminus and having a molecular mass of 22255 Dalton. GH Chicken recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.3% NaHCO3 adjusted to pH 8.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SDS-PAGE gel.
    (b) Analysis by SEC-HPLC.

    Biological Activity

    GH Chicken Recombinantis fully biologically active in homologous assays and in PDF-P1 3B9 cells stably transfected with rabbit GH receptors.

    More Info

    • Introduction

      GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five GHs, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH 1,

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH Chicken although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and filter sterilization GH can be stored at 4°C for several weeks. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is recommended.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GH Chicken Recombinant in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml and not more than 3 mg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Phe-Pro-Ala.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.75 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0 This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GH as a Reference Standard.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Growth Hormone Chicken
  • View Data Sheet

    Name :

    Follicle Stimulating Hormone Human

    Description:

    Human Follicle Stimulating Hormone

    Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.

    Product # :

    HOR-249

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    Description

    FSH Human is a glycoprotein produced from urine of post-menopausal women and having a total molecular mass of 30,000 Dalton.FSH is a heterodimeric hormone consisting of 92 amino acids a chain and 111 amino acids b chain.The FSH is purified by proprietary chromatographic techniques.

    Source

    Urine of post-menopausal women.

    Formulation

    The FSH was lyophilized with no additives.

    More Info

    • Introduction

      Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproductionIn women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production.
      In men, FSH enhances the production of androgen-binding proteinby the Sertoli cells of the testes and is critical for spermatogenesis.
      In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle.
      Like its partner, LH, FSH release at the pituitary gland is controlled by pulses of gonadotropin-releasing hormone(GnRH). Those pulses, in turn, are subject to the estrogen feed-back from the gonads.

    • Synonyms

      Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH-beta should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Follicle Stimulating Hormone in sterile pyrogen free water at 2,000IU/1ml, which can then be further diluted to other aqueous solutions.

    • Background

      What is the molecular weight/Mw of FOLLICLE STIMULATING HORMONE HUMAN Protein?
      FOLLICLE STIMULATING HORMONE HUMAN Protein has a total Mw of 30kDa.

      What is the source or expression system of FOLLICLE STIMULATING HORMONE HUMAN Protein?
      Urine of post-menopausal women.

      What is the Biological Activity of FOLLICLE STIMULATING HORMONE HUMAN Protein?
      The biological functionality of FOLLICLE STIMULATING HORMONE HUMAN Protein will be determined in the future.

      What is the amino acid sequence of FOLLICLE STIMULATING HORMONE HUMAN Protein?
      FOLLICLE STIMULATING HORMONE HUMAN Protein is composed from 92 amino acids a chain and 111 amino acids b chain.

      What applications can FOLLICLE STIMULATING HORMONE HUMAN Protein be used in?
      FOLLICLE STIMULATING HORMONE HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FOLLICLE STIMULATING HORMONE HUMAN Protein?
      The endotoxin level is minimal, FOLLICLE STIMULATING HORMONE HUMAN Protein was purified using conventional chromatography techniques.


    • Contaminants

      Less than: 0.1% hCG, 0.5%TSH, 0.5% LH, 0.5%GH and 0.5%Prl.Free of HbsAg, antibodies to HIV and HCV.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Fsh Human
  • View Data Sheet

    Name :

    Calumenin Human

    Description:

    Calumenin Human Recombinant

    CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.

    Product # :

    PRO-2465

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    Description

    Calumenin Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (20-315) and having a molecular mass of 35kDa. Calumenin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Calumenin solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The IC50 value is < 2.0nM. The inhibitory function of Cystatin 5 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.

    More Info

    • Introduction

      Calumenin is a calcium-binding protein located in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Calumenin binds 7 calcium ions having low affinity and takes part in such ER functions as protein folding and sorting.

    • Synonyms

      CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MKPTEKKDRV HHEPQLSDKV HNDAQSFDYD HDAFLGAEEA KTFDQLTPEE SKERLGKIVS KIDGDKDGFV TVDELKDWIK FAQKRWIYED VERQWKGHDL NEDGLVSWEE YKNATYGYVL DDPDPDDGFN YKQMMVRDER RFKMADKDGD LIATKEEFTA FLHPEEYDYM KDIVVQETME DIDKNADGFI DLEEYIGDMY SHDGNTDEPE WVKTEREQFV EFRDKNRDGK MDKEETKDWI LPSDYDHAEA EARHLVYESD QNKDGKLTKE EIVDKYDLFV GSQATDFGEA LVRHDEF.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Calumenin Human 2
  • View Data Sheet

    Name :

    CXCL4 Variant 1 Human

    Description:

    Platelet Factor-4 Variant 1 Human Recombinant

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-243

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    Description

    CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cxcl4 Variant 1
  • View Data Sheet

    Name :

    Leptin Dog

    Description:

    Leptin Dog Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-506

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    Description

    Leptin Dog Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Leptin Dog
  • View Data Sheet

    Name :

    Angiotensin

    Description:

    Angiotensin

    Angiotensinogen, Serpin A8, ANHU, SERPINA8.

    Product # :

    ENZ-283

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    Description

    Angiotensin contains a total of 8 amino acids having a molecular weight of 1031.2 Dalton and a molecular formula of C49H70N14O11.

    Source

    Synthetic.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Angiotensin is an oligopeptide in the blood that causes vasoconstriction, increased blood pressure, and release of aldosterone from the adrenal cortex. It is a powerful dipsogen. It is derived from the precursor molecule angiotensinogen, a serum globulin produced in the liver. It plays an important role in the renin-angiotensin system.
      The protein encoded by this gene, pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and is cleaved by the enzyme renin in response to lowered blood pressure. The resulting product, angiotensin I is then cleaved by angiotensin converting enzyme (ACE) to generate the physiologically active enzyme angiotensin II. The protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia.

    • Synonyms

      Angiotensinogen, Serpin A8, ANHU, SERPINA8.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Angiotensin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serpin A8 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Angiotensin in sterile 18MΩ-cm H2O not less than 100 µg/ml or more than 10 mg/ml solutions.

    • Amino Acid Sequence

      Asn-Arg-Val-Tyr-Val-His-Pro-Phe-OH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Angiotensin
  • View Data Sheet

    Name :

    TH Mouse

    Description:

    Tyrosine Hydroxylase Mouse Recombinant

    Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.

    Product # :

    ENZ-988

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    Description

    TH Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) and having a molecular mass of 57.0kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TH protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.

    • Synonyms

      Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPMPTPSAS SPQPKGFRRA VSEQDTKQAE AVTSPRFIGR RQSLIEDARK EREAAAAAAA AAVASAEPGN PLEAVVFEER DGNAVLNLLF SLRGTKPSSL SRALKVFETF EAKIHHLETR PAQRPLAGSP HLEYFVRFEV PSGDLAALLS SVRRVSDDVR SAREDKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG EPIPHVEYTK EEIATWKEVY ATLKGLYATH ACREHLEAFQ LLERYCGYRE DSIPQLEDVS HFLKERTGFQ LRPVAGLLSA RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ FSQDIGLASL GASDEEIEKL STVYWFTVEF GLCKQNGELK AYGAGLLSSY GELLHSLSEE PEVRAFDPDT AAVQPYQDQT YQPVYFVSES FSDAKDKLRN YASRIQRPFS VKFDPYTLAI DVLDSPHTIR RSLEGVQDEL HTLTQALSAI SHHHHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Th Mouse
  • View Data Sheet

    Name :

    Leptin Bovine

    Description:

    Leptin Bovine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-502

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    Description

    Leptin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Leptin Bovine
  • View Data Sheet

    Name :

    CMV Pp65

    Description:

    Cytomegalo Virus Pp65 (UL83) Recombinant

    Product # :

    CMV-215

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    Description

    The E.Coli derived 52.2 kDa recombinant protein contains the CMV Pp65 (UL83) immunodominant regions, 297-510 amino acids. Recombinant CMV-Pp65 is fused to a 26 kDa GST tag.

    Source

    Escherichia Coli.

    Formulation

    CMV PP65 protein solution is supplied in PBS.

    Purity

    CMV Pp65 protein is >90% pure as determined by SDS-PAGE.

    More Info

    • Introduction

      CMV belongs to the Betaherpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.

    • Stability

      CMV Pp65 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      CMV Pp65 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.

    • Specificity

      Strongly reacts with human CMV positive serum.

    • Purification Method

      CMV Pp65 was purified by proprietary chromatographic technique.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cmv Pp65
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