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  • Cytokines
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  • Chemokines
  • Cd antigens
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  • 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

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  • BCA-1/ BLC (CXCL13)

    BCA-1/ BLC (CXCL13)

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    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

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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

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    CD1

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    CD2

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    CD200

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    CD207

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    CD226

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    CD23

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    CD244

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    CD247

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    CD27

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    CD274

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    CD300

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    CD33

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  • Beta-NGF

    Beta-NGF

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    Glia Maturation Factor

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    MANF

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    Neuroglobin

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  • Neuregulin

    Neuregulin

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    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

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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

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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

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    Hydrolase

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  • Phosphatase

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    Adenylate Kinase

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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

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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 “syntaxin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    SARS Envelope, His

    Description:

    SARS-Associated Coronavirus Envelope Recombinant, His Tag

    Product # :

    SARS-004

    Price :

    Quantity :

    Shipping Method :

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    Description

    The E.coli derived recombinant protein contains the Envelope protein 1-76 amino acids immunodominant regions fused to 6xHis tag at C-terminal.

    Source

    Escherichia Coli.

    Formulation

    SARS Envelope protein solution is supplied in PBS.

    Purity

    Protein is >90% pure as determined SDS-PAGE.

    More Info

    • Introduction

      SARS Associated Coronavirus Envelope is a small membrane protein that takes major part in the life cycle of the virus. This protein is needed for the assembly, budding, creation of the envelope and pathogenesis. This protein contains 3 outer structural proteins, the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to assure viral entry thetarget cells. Accordingly, S-protein has a major part in virus infection cycle and is the mainly target of neutralizing antibodies.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Protein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Specificity

      Immunoreactive with sera of SARS-infected individuals.

    • Purification Method

      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.

    product_image.jpg
  • View Data Sheet

    Name :

    Bartonella SucB

    Description:

    Bartonella Henselae SucB Recombinant

    Product # :

    PRO-2570

    Price :

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    Description

    Recombinant Bartonella Henselae SucB produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 48kDa. Bartonella SucB is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bartonella SucB is supplied at a 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Numerous forms of Bartonellosis are caused by Bartonella henselae as well as Cat Scratch Disease & Bacillary Angiomatosis. It has been found that up to 95% of patients with Cat Scratch Disease show antibodies against Bartonella henselae antigens. Highly immunoreactive proteins which are produced by the Bartonella henselae are the most important antigens used for the diagnosis of Cat Scratch Disease. The immunogenic protein dihydrolipoamide-succinyltransferase also named SucB is an enzyme of the alpha-ketoglutarate dehydrogenase complex, which catalyzes the transport of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A.

    • Physical Appearance

      Sterile Filtered 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. Avoid multiple 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.

    Bartonella Henselae Sucb
  • View Data Sheet

    Name :

    Clusterin Antibody

    Description:

    Clusterin, Mouse Anti Human

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

    Product # :

    ANT-314

    Price :

    Quantity :

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    • formulation
    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol & 0.02% Sodium Azide.

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified. The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the ? and ? chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil ? -helices and three predicted amphipathic a-helices. Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen. It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, b

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human Clusterin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Clusterin amino acids 1-333 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P1A11AT.

    • Applications

      Clusterin antibody has been tested by ELISA, Western blot, ICC/IF, IHC and FACS analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      Clusterin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Clusterin Antibody
  • View Data Sheet

    Name :

    NPPA Human

    Description:

    Natriuretic Peptide A Human Recombinant

    Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND. 

    Product # :

    CYT-1028

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    Description

    NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.

    • Synonyms

      Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.

    • 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. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.

    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.

    Nppa Human
  • View Data Sheet

    Name :

    CTSL Mouse

    Description:

    Cathepsin-L Mouse Recombinant

    Cathepsin L1, Cathepsin L, Major excreted protein, MEP, p39 cysteine proteinase.

    Product # :

    ENZ-944

    Price :

    Quantity :

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    Description

    CTSL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (18-334a.a.) and having a molecular mass of 36.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTSL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTSL 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

      Cathepsin-L also known as CTSL is a member of the peptidase C1 family. CTSL, is a dimer composed of disulfide-linked heavy and light chains, both formed from a single protein precursor. Furthermore, CTSL is a lysosomal cysteine proteinase which takes a main part in intracellular protein catabolism. CTSL substrates include collagen and elastin, as well as alpha-1 protease inhibitor, which is the most important controlling element of neutrophil elastase activity. CTSL has been implicated in a number of pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. Multiple alternatively spliced transcript variants have been found for CTSL.

    • Synonyms

      Cathepsin L1, Cathepsin L, Major excreted protein, MEP, p39 cysteine proteinase.

    • 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

      TPKFDQTFSA EWHQWKSTHR RLYGTNEEEW RRAIWEKNMR MIQLHNGEYS NGQHGFSMEM NAFGDMTNEE FRQVVNGYRH QKHKKGRLFQ EPLMLKIPKS VDWREKGCVT PVKNQGQCGS CWAFSASGCL EGQMFLKTGK LISLSEQNLV DCSHAQGNQG CNGGLMDFAF QYIKENGGLD SEESYPYEAK DGSCKYRAEF AVANDTGFVD IPQQEKALMK AVATVGPISV AMDASHPSLQ FYSSGIYYEP NCSSKNLDHG VLLVGYGYEG TDSNKNKYWL VKNSWGSEWG MEGYIKIAKD RDNHCGLATA ASYPVVNLEH HHHHH.

    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.

    Ctsl Mouse
  • View Data Sheet

    Name :

    BLyS Human, Plant

    Description:

    BAFF (BLyS) Human Recombinant, Plant

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-054

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
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    Description

    BAFF human Recombinant produced in Nicotiana benthamiana plant is a single glycosilated polypeptide chain containing 151 amino acids fragment (134-285).BAFF (C830H1277N223O242S5) is fused to a 10-His-tag at the N-terminal having the total molecular mass of 18-20kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 20 mM PBS buffer pH 7 and 0.2 M NaCl.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
    *activity results may vary with PBMC donors.
    ED50 ? 50ng/ml

    More Info

    • Introduction

      BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity.A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF 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 BAFF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 19kDa.

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

      What is the Purity of BLYS Protein?
      BLYS Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BLYS Protein?
      The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.

      What is the amino acid sequence of BLYS Protein?
      HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL

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

      What is the endotoxin level for BLYS Protein?
      The endotoxin level is minimal, BLYS 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.

    Baff Human Plant
  • View Data Sheet

    Name :

    Hirudin

    Description:

    Hirudin Recombinant

    Product # :

    PRO-362

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    Description

    Recombinant Hirudin is derived from yeast and the polypeptide chain contains 65 amino acids and its Mw is 6979.5 Dalton which is identical to natural Hirudin except for the substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63.The Recombinant Hirudin is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Each mg of protein was lyophilized from a sterile solution containing 20mM PBS pH-7 and 2% mannitol.

    Purity

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

    Biological Activity

    The specific activity was found to be >14,000ATU/mg.

    More Info

    • Introduction

      Recombinant Hirudin is a potent thrombin inhibitor originally derived from the medicinal leech. Hirudin acts directly on thrombin rather than through other clotting factors. The mechanism of Hirudin-thrombin appears to be unique. The conversion of fibrinogen into fibrin by the serine protease enzyme thrombin is a major event in the final stages of blood coagulation. In the final stages of coagulation prothrombinase converts prothrombin into thrombin. Fibrin is subsequently cross linked by factor XIII to form a blood clot. The primary inhibitor of thrombin in normal blood circulation is antithrombin III. The anticoagulatant activity of hirudin is derived from its ability to inhibit the pro-coagulant activity of thrombin (similar to antithrombin III activity). Hirudin is the strongest natural inhibitor of thrombin. Hirudin binds to and inhibits only the activity of thrombin forms with a specific activity on fibrinogen contrasting to antithrombin III activity. Therefore, hirudin has a thrombolytic activity since it prevents or dissolves the formation of clots and thrombi. Hirudin also has therapeutic significance in blood coagulation disorders, in the treatment of skin hematomas and of superficial varicose veins. Hirudin does not hinder with the biological activity of other serum proteins and can also act on complexed thrombin, thus having an advantage over more common anticoagulants and thrombolytics. It is complicated to extract large quantities of hirudin from natural sources; therefore a method for producing and purifying hirudin using recombinant biotechnology has been developed.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Hirudin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hirudin 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 Hirudin 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.

    Hirudin
  • View Data Sheet

    Name :

    Leptin qA Mouse, Antagonist

    Description:

    Leptin Quadruple Antagonist Mouse Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1257

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    Description

    Leptin Quadruple Antagonist Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino, an additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. The Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. Leptin Quadruple Antagonist Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Quadruple Antagonist Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Mouse Leptin Quadruple Antagonist also inhibits various leptin effects in several in vitro bioassays. The inhibitory activity of Mouse Leptin Quadruple Antagonist was increased 14 to 60 fold as measured by various criteria such as binding properties to human leptin binding domain and in vitro and in vivo bioassays as compared to mouse leptin antagonist.

    More Info

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Quadruple 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 LEP Antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted 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 of mouse super-active leptin antagonist was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Background

      Leptin is produced by adipocytes and its main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene and effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours 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 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 Mouse Antagonist
  • View Data Sheet

    Name :

    Leptin Super Antagonist Human

    Description:

    Leptin Super Antagonist Human Recombinant

    Product # :

    CYT-1238

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    Description

    Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Super Leptin Antagonist 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-Gln.

    • Background

      Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

    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 Antagonist Super Human
  • View Data Sheet

    Name :

    AKR7A3, Human

    Description:

    Aldo-Keto Reductase Family 7 Member A3 Human Recombinant

    AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    Product # :

    ENZ-1129

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    Description

    AKR7A3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-331) and having a molecular mass of 37.7 kDa.AKR7A3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR7A3 solution (1mg/ml) contains 10% Glycerol and 20mM Tris-HCl buffer (pH 8.5).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 800pmol/min/ug. It is defined by the amount of enzyme that catalyzes the reduction 1.0pmole of 1,2-Naphthoquinone presence of NADPH per minute at pH 7.0 at 25˚C.

    More Info

    • Introduction

      Aldo-Keto Reductase Family 7 Member A3 or AKR7A3, is an enzyme, it is part of the detoxification of aldehydes and ketones process. AKR7A3 diminishes the dialdehyde protein-binding form of aflatoxin B1 to the non-binding AFB1 dialcohol. The enzyme takes partin protection of liver from toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

    • Synonyms

      AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    • 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

      MSRQLSRARP ATVLGAMEMG RRMDAPTSAA VTRAFLERGH TEIDTAFVYS EGQSETILGG LGLRLGGSDC RVKIDTKAIP LFGNSLKPDS LRFQLETSLK RLQCPRVDLF YLHMPDHSTP VEETLRACHQ LHQEGKFVEL GLSNYAAWEV AEICTLCKSN GWILPTVYQG MYNAITRQVE TELFPCLRHF GLRFYAFNPL AGGLLTGKYK YEDKDGKQPV GRFFGNTWAE MYRNRYWKEH HFEGIALVEK ALQAAYGASA PSMTSATLRW MYHHSQLQGA HGDAVILGMS SLEQLEQNLA AAEEGPLEPA VVDAFNQAWH LVAHECPNYF R

    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.

    Akr7A3 Enzyme
  • View Data Sheet

    Name :

    SUMO1 Human

    Description:

    SUMO1 Human Recombinant

    Small ubiquitin-related modifier 1, SUMO-1, Sentrin, Ubiquitin-like protein SMT3C, SMT3 homolog 3, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein UBL1, GAP-modifying protein 1, GMP1, SUMO1, SMT3C, SMT3H3, UBL1, PIC1, SMT3, DAP-1, OFC10, SENP2.

    Product # :

    PRO-326

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    Description

    The active human SUMO-I (the 1-97 animo acid region of the Ubiquitin-like protein SMT3C precursor). The enzyme contains a single polypeptide band of 11 kDa. The predicted molecular weight of hSOMO I is 11 kDa. The The final fraction of enzyme contains single polypeptide band of approximately 20 kDa on SDS PAGE.

    Source

    Escherichia Coli.

    Formulation

    10mM sodium chloride, 100mM imidazole, 0.5mM PMSF, 1mM DTT and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      SUMO1 is a protein that belongs to the SUMO (small ubiquitin-like modifier) protein family. SUMO1 functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. Still, unlike ubiquitin which targets proteins for degradation, SUMO1 is involved in a variety of cellular processes, for example nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO1 is not active until the last four amino acids of the carboxy-terminus are cleaved off.

    • Synonyms

      Small ubiquitin-related modifier 1, SUMO-1, Sentrin, Ubiquitin-like protein SMT3C, SMT3 homolog 3, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein UBL1, GAP-modifying protein 1, GMP1, SUMO1, SMT3C, SMT3H3, UBL1, PIC1, SMT3, DAP-1, OFC10, SENP2.

    • 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.

    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.

    Sumo1 Human
  • View Data Sheet

    Name :

    PRKACA Human, sf9

    Description:

    c-AMP dependant Protein Kinase A catalytic subunit alpha Human Recombinant, Sf9

    cAMP-dependent protein kinase alpha-catalytic subunit, EC 2.7.11.11, PKA C-alpha, PKACA, PRKACA,  MGC48865, MGC102831.

    Product # :

    PKA-093

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    Description

    PRKACA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 578 amino acids (1-351 a.a.) and having a molecular mass of 67kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). PRKACA is expressed with a 227 amino acid GST Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      cAMP-dependent protein kinase catalytic subunit alpha isoform Calpha1 (PRKACA) belongs to the Ser/Thr protein kinase family. PRKACA is responsible for phosphorylating other proteins and substrates, changing their activity. The PRKACA protein is a member of the AGC kinase family, and contributes to the regulation of cellular processes which include glucose metabolism, cell division, and contextual memory.

    • Synonyms

      cAMP-dependent protein kinase alpha-catalytic subunit, EC 2.7.11.11, PKA C-alpha, PKACA, PRKACA, MGC48865, MGC102831.

    • 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

      MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSHMGN AAAAKKGSEQ ESVKEFLAKA KEDFLKKWES PAQNTAHLDQ FERIKTLGTG SFGRVMLVKH KETGNHYAMK ILDKQKVVKL KQIEHTLNEK RILQAVNFPF LVKLEFSFKD NSNLYMVMEY VPGGEMFSHL RRIGRFSEPH ARFYAAQIVL TFEYLHSLDL IYRDLKPENL LIDQQGYIQV TDFGFAKRVK GRTWTLCGTP EYLAPEIILS KGYNKAVDWW ALGVLIYEMA AGYPPFFADQ PIQIYEKIVS GKVRFPSHFS SDLKDLLRNL LQVDLTKRFG NLKNGVNDIK NHKWFATTDW IAIYQRKVEA PFIPKFKGPG DTSNFDDYEE EEIRVSINEK CGKEFSEF.

    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.

    Prkaca Human Sf9
  • View Data Sheet

    Name :

    ATP5D Human

    Description:

    ATP Synthase Subunit D, Mitochondrial Human Recombinant

    ATP synthase subunit delta mitochondrial, F-ATPase delta subunit, ATP5D.

    Product # :

    ENZ-143

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    Description

    ATP5D produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (23-168 a.a.) and having a molecular mass of 17.3kDa.ATP5D is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ATP5D protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      F-ATPase delta (ATP5D) catalyzes ATP synthesis, employing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of 2 linked multi-subunit complexes: F1-the soluble catalytic core and Fo- the membrane-spanning component, which comprise the proton channel. The catalytic portion of mitochondrial ATP synthase consists of five different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alphas, 3 betas, and a single representative of the other three. The proton channel consists of three main subunits-a, b, c. ATP5D is the delta subunit of the catalytic core.

    • Synonyms

      ATP synthase subunit delta mitochondrial, F-ATPase delta subunit, ATP5D.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      ATP5D Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAEAAAAPAA ASGPNQMSFT FASPTQVFFN GANVRQVDVP TLTGAFGILA AHVPTLQVLR PGLVVVHAED GTTSKYFVSS GSIAVNADSS VQLLAEEAVT LDMLDLGAAK ANLEKAQAEL VGTADEATRA EIQIRIEANE ALVKALE.

    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.

    Atp5D Human
  • View Data Sheet

    Name :

    IFN a 2b Human

    Description:

    IFN-Alpha 2b Human Recombinant

    IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

    Product # :

    CYT-205

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    Description

    IFN-a 2b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids and having a molecular mass of 19400 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine. The IFN-alpha 2b gene was obtained from human leukocytes. The IFN-a 2b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.

    Purity

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

    Biological Activity

    The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

    More Info

    • Introduction

      IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

    • Synonyms

      IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN alpha 2b 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 IFN-alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE

    • Background

      IFN-alpha forms are produced by monocytes/macrophages, lymphoblastoid cells, fibroblasts, and a number of different cell types following induction by viruses, nucleic acids, glucocorticoid hormones, and low-molecular weight substances (n-butyrate, 5-bromodeoxy uridine). At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. Disulfide bonds are formed between cysteines at positions 1/98 and 29/138. The disulfide bond 29/138 is essential for biological activity while the 1/98 bond can be reduces without affecting biological activity. All IFN-alpha forms contain a potential glycosylation site but most subtypes are not glycosylated. In contrast to IFN-gamma IFN-alpha proteins are stable at pH2.

      There are at least 23 different IFN-alpha genes. They have a length of 1-2 kb and are clustered on human chromosome 9p22. It is not known whether all these genes are expressed following stimulation of the cells. In some cell systems expression of some subtypes (IFN-alpha-1, IFN-alpha-2, IFN-alpha-4) is stronger than those of others. IFN-alpha genes do not contain intron sequences found in many other eukaryotic genes (see also: gene expression). Based upon the structures two types of IFN-alpha genes, designated class 1 and II, are distinguished. They encode proteins of 156-166 and172 amino acids, respectively. Deletions covering 9p22 are observed frequently in cells of lymphoblastoid leukemias. It is not known to date whether this is of significance with respect to IFN expression.

      The gene encoding the IFN-alpha receptor maps to human chromosome 21q22.1. IFN-alpha and IFN-beta are thought to bind to the same IFN binding subunit which is expressed in 100-5000 copies in IFN-alpha sensitive and -resistant cells and is associated with other as yet unidentified proteins. The IFN-omega (Omega IFN) also binds to the IFN-alpha/IFN-beta receptor. Another receptor expressed on B-lymphocytes is identical with CD21. This receptor also binds Epstein-Barr virus through its gp350/220 coat protein.Signal transduction mechanisms elicited after binding of IFN-alpha to its receptors involves tyrosine phosphorylation (see also: PTK; protein tyrosine kinase) of various non-receptor tyrosine kinases belonging to the Janus kinases. Soluble forms of the IFN-alpha receptor, corresponding to truncated forms of the extracellular domain of the cell surface IFN-alpha receptor, have been found in human serum and in normal human urine.

      All known subtypes of IFN-alpha show the same antiviral antiparasitic, antiproliferative activities in suitable bioassays although they may differ in relative activities. Human IFN-alpha is also a potent antiviral substance in murine, porcine, and bovine cell systems. Human IFN-alpha is less active in rodent cells. Site-directed mutagenesis techniques have been used to create some variants of certain subtypes (IFN-alpha-2) that display approximately 100-fold enhanced antiviral activities in mouse cells.

      What is the molecular weight/Mw of IFN A 2B HUMAN Protein?
      IFN A 2B HUMAN Protein has a total Mw of 19.4kDa.

      What is the source or expression system of IFN A 2B HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IFN A 2B HUMAN Protein?
      IFN A 2B HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFN A 2B HUMAN Protein?
      The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

      What is the amino acid sequence of IFN A 2B HUMAN Protein?
      MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
      What applications can IFN A 2B HUMAN Protein be used in?
      IFN A 2B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFN A 2B HUMAN Protein?
      The endotoxin level is minimal, IFN A 2B HUMAN Protein was purified using conventional chromatography techniques.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.924 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). 2. Analysis by RP-HPLC, using a calibrated solution of IFN alpha 2b 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.

    Interferon Alpha 2B Human
  • View Data Sheet

    Name :

    CTF1 Human, His

    Description:

    Cardiotrophin-1 Human Recombinant, His Tag

    CTF1, CT1, CT-1, Cardiophin 1.

    Product # :

    CYT-436

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    Description

    The Cardiotrophin His-Tagged Fusion Protein Human, produced in E. coli, is 22.5 kDa protein containing 200 amino acid residues of the human Cardiotrophin and 12 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    CTF1 was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Purity of CTF1 Human Recombinant is greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
      CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
      Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
      Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.

    • Synonyms

      CTF1, CT1, CT-1, Cardiophin 1.

    • 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 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/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 10?g/ml. In higher concentrations the solubility of this antigen is limited. Protein is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GSSRREGSLE DPQTDSSVSL LPHLEAKIRQ THSLAHLLTK YAEQLLQEYV QLQGDPFGLPSFSPPRLPVA GLSAPAPSHA GLPVHERLRL DAAALAALPP LLDAVCRRQA ELNPRAPRLL RRLEDAARQA RALGAAVEAL LAALGAANRG PRAEPPAATA SAASATGVFP AKVLGLRVCG LYREWLSRTE GDLGQLLPGG SA.

    • Background

      What is the molecular weight/Mw of CTF1 Protein?
      CTF1 Protein has a total Mw of 22.5kDa.

      What is the source or expression system of CTF1 Protein?
      Escherichia Coli.

      What is the Purity of CTF1 Protein?
      CTF1 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF1 Protein?
      The biological functionality of CTF1 Protein will be determined in the future.

      What is the amino acid sequence of CTF1 Protein?
      MRGSHHHHHH GSSRREGSLE DPQTDSSVSL LPHLEAKIRQ THSLAHLLTK YAEQLLQEYV QLQGDPFGLPSFSPPRLPVA GLSAPAPSHA GLPVHERLRL DAAALAALPP LLDAVCRRQA ELNPRAPRLL RRLEDAARQA RALGAAVEAL LAALGAANRG PRAEPPAATA SAASATGVFP AKVLGLRVCG LYREWLSRTE GDLGQLLPGG SA.

      What applications can CTF1 Protein be used in?
      CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF1 Protein?
      The endotoxin level is minimal, CTF1 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.

    Cardiotrophin 1 Human
  • View Data Sheet

    Name :

    CTLA4 Human, igG-His

    Description:

    Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant, igG-His Tag

    CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.

    Product # :

    CYT-985

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    Description

    CTLA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 368 amino acids (36-161a.a.) and having a molecular mass of 40.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTLA4 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTLA4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.

    • Synonyms

      CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.

    • 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

      ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

    • Background

      What is the molecular weight/Mw of CTLA4 Protein?
      CTLA4 Protein has a total Mw of 40.8kDa.

      What is the source or expression system of CTLA4 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CTLA4 Protein?
      CTLA4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTLA4 Protein?
      The biological functionality of CTLA4 Protein will be determined in the future.

      What is the amino acid sequence of CTLA4 Protein?
      ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

      What applications can CTLA4 Protein be used in?
      CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTLA4 Protein?
      The endotoxin level is minimal, CTLA4 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.

    Ctla4 Human Igg His
  • View Data Sheet

    Name :

    LGALS8 Human, His

    Description:

    Galectin-8 Human Recombinant, His Tag

    Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

    Product # :

    CYT-727

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    • SDS-PAGE

    Description

    LGALS8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-317 a.a.) and having a molecular mass of 37.9 kDa. The LGALS8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-8 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 10% glycerol & 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.

    SDS-PAGE

    LGALS8 Human, His-SDS-PAGE - Product image 1

    More Info

    • Introduction

      LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.

    • Synonyms

      Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

    • 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

      MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
      KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
      QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
      EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

    • Background

      What is the molecular weight/Mw of LGALS8 HUMAN, HIS Protein?
      LGALS8 HUMAN, HIS Protein has a total Mw of 37.9kDa.

      What is the source or expression system of LGALS8 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of LGALS8 HUMAN, HIS Protein?
      LGALS8 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS8 HUMAN, HIS Protein?
      The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.What is the amino acid
      sequence of LGALS8 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
      KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
      QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
      EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

      What applications can LGALS8 HUMAN, HIS Protein be used in?
      LGALS8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS8 HUMAN, HIS Protein?
      The endotoxin level is minimal, LGALS8 HUMAN, HIS 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.

    Lgals8 Human His
  • View Data Sheet

    Name :

    HINT2 Human

    Description:

    Histidine Triad Nucleotide Binding Protein 2 Human Recombinant

    Histidine triad nucleotide-binding protein 2 mitochondrial, HINT-2, HINT-3 HIT-17kDa, PKCI-1-related HIT protein, HINT2, histidine triad nucleotide binding protein 2, HIT-17.

    Product # :

    PRO-1455

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    Description

    HINT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (18-163 a.a) and having a molecular mass of 17.9kDa.HINT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HINT2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Histidine triad nucleotide-binding protein 2 (HINT2) belongs to the triad proteins, which are nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides. Hydrolase is most likely involved in steroid biosynthesis, furthermore it might play a role in apoptosis. HINT2 shows high expression in liver and pancreas. Expression is significantly down-regulated in hepatocellular carcinoma (HCC) patients.

    • Synonyms

      Histidine triad nucleotide-binding protein 2 mitochondrial, HINT-2, HINT-3 HIT-17kDa, PKCI-1-related HIT protein, HINT2, histidine triad nucleotide binding protein 2, HIT-17.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSVAATGVR GGQVRGAAGV TDGNEVAKAQ QATPGGAAPT IFSRILDKSL PADILYEDQQ CLVFRDVAPQ APVHFLVIPK KPIPRISQAE EEDQQLLGHL LLVAKQTAKA EGLGDGYRLV INDGKLGAQS VYHLHIHVLG GRQLQWPPG.

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    Hint2 Human
  • View Data Sheet

    Name :

    SCGB2A2 Human, HEK

    Description:

    Mammaglobin-A Human Recombinant, HEK

    Mammaglobin-A, Mammaglobin-1, Secretoglobin family 2A member 2, SCGB2A2, MGB1, UGB2, MGC71974.

    Product # :

    PRO-2038

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    Description

    Mammaglobin-A Human Recombinant (Fc Chimera) produced in HEK cells is a single, glycosylated, polypeptide chain (Gly19-Phe93) containing a total of 321 amino acids, having a calculated molecular mass of 36.3kDa. The SCGB2A2 protein is fused to a 2 aa C-terminal linker, a 6 aa C-terminal His tag, a 7 aa TEV site and a 231 aa Human IgG1 fragment (Pro100-Lys330).

    Source

    HEK 293.

    Formulation

    SCGB2A2 was filtered (0,4µm) and lyophilized from 0.5mg/ml in PBS buffer and 5% (w/v) Threalose pH 7.4

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The mammaglobin gene was first identified using a differential screening approach directed at the isolation of novel, human breast cancer-associated genes. Mammaglobin encodes a 10 kDa glycoprotein and is distantly relaetd to a family of epithelial secretory proteins that includes rat estramustine-binding protein/prostatein and human Clara cell 10 kDa protein (CC10)/uteroglobin. Mammaglobin, a mammary-specific member of the uterglobin family, is known to be overexpressed in human breast cancer. Studies suggest that mammaglobin is one of the first relatively mammary-specific and mammary-sensitive markers (85%). Mammaglobin may be valuable used in a panel with BRST-2 (GCDFP-15) and ER in evaluating tumors of unknown primary sites.
      SCGB2A2 (the mammaglobin gene) is located on chromosome 11, at locus 11q13. SCGB2A2 is member of the secretoglobin superfamily of which is a group of small dimeric secreted and sometimes glycosylated proteins. Expressed mainly in mucosa, secretoglobins appear to be involved in cell signalling, immune response, chemotaxis, and might also serve as transporters for steroid hormones in humans.

    • Synonyms

      Mammaglobin-A, Mammaglobin-1, Secretoglobin family 2A member 2, SCGB2A2, MGB1, UGB2, MGC71974.

    • Physical Appearance

      Sterile filtered lyophilized 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 5 days.

    • 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

      GSGCPLLENV ISKTINPQVS KTEYKELLQE FIDDNATTNA IDELKECFLN QTDETLSNVE VFMQLIYDSS LCDLF KLENL YFQGPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

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    Scgb2A2 Human Hek
  • View Data Sheet

    Name :

    ALCAM (CD166) Mouse

    Description:

    Activated Leukocyte Cell Adhesion Molecule (CD166) Mouse Recombinant

    Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

    Product # :

    PRO-2749

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    Description

    ALCAM mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 739 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa. ALCAM is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ALCAM protein solution (0.25mg/ml) contains 50% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to block the adhesion of Jurkat human acute T cell leukemia cells to immobilized Recombinant Human CD6. When cells are added to 1 ug/ml of mouse ALCAM binded to CD6, this effect is more to 50%.

    More Info

    • Introduction

      CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.

    • Synonyms

      Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

    • 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

      WYTVNSAYGD TIVMPCRLDV PQNLMFGKWK YEKPDGSPVF IAFRSSTKKS VQYDDVPEYK DRLSLSENYT LSIANAKISD EKRFVCMLVT EDNVFEAPTL VKVFKQPSKP EIVNKAPFLE TDQLKKLGDC ISRDSYPDGN ITWYRNGKVL QPVEGEVAIL FKKEIDPGTQ LYTVTSSLEY KTTRSDIQMP FTCSVTYYGP SGQKTIYSEQ EIFDIYYPTE QVTIQVLPPK NAIKEGDNIT
      LQCLGNGNPP PEEFMFYLPG QPEGIRSSNT YTLTDVRRNA TGDYKCSLID KRNMAASTTI TVHYLDLSLN PSGEVTKQIG DTLPVSCTIS ASRNATVVWM KDNIRLRSSP SFSSLHYQDA GNYVCETALQ EVEGLKKRES LTLIVEGKPQ IKMTKKTDPS GLSKTIICHV EGFPKPAIHW TITGSGSVIN QTEESPYING RYYSKIIISP EENVTLTCTA ENQLERTVNS LNVSAISIPE
      HDEADDISDE NREKVNDQAK LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK HHHHHH

    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.

    Cd166 Mouse
  • View Data Sheet

    Name :

    ARMC10 Human

    Description:

    Armadillo Repeat Containing 10 Human Recombinant

    Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    Product # :

    PRO-1453

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    Description

    ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.

    • Synonyms

      Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.

    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.

    Armc10 Human
  • View Data Sheet

    Name :

    IFNA7 Human, Sf9

    Description:

    Interferon-alpha 7 Human Recombinant, Sf9

    Interferon alpha-7, IFN-alpha-7, Interferon alpha-J, LeIF J, Interferon alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.

    Product # :

    CYT-1075

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    • SDS-PAGE

    Description

    IFNA7 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 175 amino acids (24-189) and having a molecular mass of 20.7kDa. IFNA7 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IFNA7 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    SDS-PAGE

    IFNA7 Human, Sf9 - Product image 1

    More Info

    • Introduction

      Interfereon alpha 7 (IFNA7) is a member of the alpha/beta interferon family. IFNA7 is generated by macrophages. IFN-alpha has antiviral functions. Interferon promotes the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.

    • Synonyms

      Interferon alpha-7, IFN-alpha-7, Interferon alpha-J, LeIF J, Interferon alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.

    • 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

      ADPCDLPQTH SLRNRRALIL LAQMGRISPF SCLKDRHEFR FPEEEFDGHQ FQKTQAISVL HEMIQQTFNL FSTEDSSAAW EQSLLEKFST ELYQQLNDLE ACVIQEVGVE ETPLMNEDFI LAVRKYFQRI TLYLMEKKYS PCAWEVVRAE IMRSFSFSTN LKKGLRRKDH HHHHH.

    • Background

      What is the molecular weight/Mw of IFNA7 HUMAN, SF9 Protein?
      IFNA7 HUMAN, SF9 Protein has a total Mw of 20.7kDa.

      What is the source or expression system of IFNA7 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IFNA7 HUMAN, SF9 Protein?
      IFNA7 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNA7 HUMAN, SF9 Protein?
      The biological functionality of IFNA7 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of IFNA7 HUMAN, SF9 Protein?
      ADPCDLPQTH SLRNRRALIL LAQMGRISPF SCLKDRHEFR FPEEEFDGHQ FQKTQAISVL HEMIQQTFNL FSTEDSSAAW EQSLLEKFST ELYQQLNDLE ACVIQEVGVE ETPLMNEDFI LAVRKYFQRI TLYLMEKKYS PCAWEVVRAE IMRSFSFSTN LKKGLRRKDH HHHHH.

      What applications can IFNA7 HUMAN, SF9 Protein be used in?
      IFNA7 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNA7 HUMAN, SF9 Protein?
      The endotoxin level is minimal, IFNA7 HUMAN, SF9 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.

    Ifna7
  • View Data Sheet

    Name :

    SRP54 Human

    Description:

    Signal Recognition Particle 54kDa Human Recombinant

    Signal Recognition Particle 54 kDa protein

    Product # :

    PRO-113

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    Description

    SRP54 is a full-length cDNA coding for the human SRP54 protein having a molecular mass of 62kDa (pH 8.9). SRP54 protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    SRP54 is supplied in 16mM HEPES buffer pH-8.0, 320mM NaCl, 5mM DTT, 1mM EDTA, 0.16mM GDP and 20% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      SRP54 is a 54-kDa subunit of the signal recognition particle (SRP), a cytoplasmic ribonucleoprotein complex which leads the translocation of newly synthesized secretory proteins from the polysome to the endoplasmic reticulum. SRP is composed of six polypeptides and a tRNA-like molecule known as 7SL RNA. SRP54 is a GTP-binding protein that directly binds the signal sequences of nascent secretory and membrane proteins. Anti-SRP autoantibodies take place in patients with an autoimmune chronic muscle inflammation called polymyositis. These auto-antibodies predominantly recognize the SRP54 subunit and in addition are able to immunoprecipitate several of the SRP subunits and the RNA component. Nearly 5% of myositis patients are positive for anti-SRP autoantibodies, increasing to 18% in the subgroup of Jo-1 autoantibody-negative patients. The classic 'anti-SRP syndrome' is a severe form of polymyositis in which the myositic inflammation is acute and aggressive onset, with common myalgias and cardiac involvement. Normally there is a poor reaction to therapy with a 5-year survival rate of about 25%.

    • Synonyms

      Signal Recognition Particle 54 kDa protein

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.5-0.9 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with myositis sera or monoclonal anti-hexa-His-tag antibody.

    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.

    Srp54 Human
  • View Data Sheet

    Name :

    PDE6H Human

    Description:

    Phosphodiesterase 6H cGMP-Specific Cone Gamma Human Recombinant

    Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.

    Product # :

    ENZ-819

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    Description

    PDE6H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (1-83 a.a) and having a molecular mass of 11.5 kDa. PDE6H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PDE6H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      PDE6H belongs to the rod/cone cGMP-PDE gamma subunit family, which selectively catalyze the hydrolysis of 3 cyclic phosphate bonds in adenosine and/or guanine 3,5 cyclic monophosphate (cAMP and/or cGMP). This family regulates the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDE6H is the inhibitory (or gamma) subunit of the cone-specific cGMP phosphodiesterase, which is atetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). PDE6H is particularly expressed in the retina, and is implicated in the transmission and amplification of the visual signal. Mutations in PDE6H have been associated with retinal cone dystrophy type 3A.

    • Synonyms

      Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMSDNTTL PAPASNQGPT TPRKGPPKFK QRQTRQFKSK PPKKGVKGFG DDIPGMEGLG TDITVICPWE AFSHLELHEL AQFGII.

    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.

    Pde6H Human
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