Skip to content

High-quality research proteins.

  • 1-800-805-6531

  • Mon - Sat 8.00-18.00, Sun - Closed

  • info@prospecbio.com

  • PO Box 6591 East Brunswick NJ 08816

  • Products
    • Cytokines
    • Growth factors
    • Chemokines
    • Cd antigens
    • Neurotrophins
    • Hormones
    • Enzymes
    • Viral antigens
    • Recombinant proteins
    • Natural proteins
    • Monoclonal antibodies
    • Polyclonal antibodies
    • Thermal Packaging
  • About
    • Company
    • Founder
    • Contribution
  • Customers
    • Eastern Asia
    • Eastern Europe
    • North America
    • South America
    • South East Asia
    • Southern Asia
    • Western Europe
  • Ordering
    • Ordering Method
    • Ordering - Credit Card
    • Ordering - PO
    • Shipping Fees
    • FAQs
  • Services
    • DNA Cloning
    • Protein Expression
    • Monoclonal Antibody
    • Fermentation
    • Technology License
  • Contact us
Log in

Country/region

  • USD $ | Albania
  • USD $ | Andorra
  • USD $ | Argentina
  • USD $ | Armenia
  • USD $ | Australia
  • USD $ | Austria
  • USD $ | Azerbaijan
  • USD $ | Belarus
  • USD $ | Belgium
  • USD $ | Bolivia
  • USD $ | Brazil
  • USD $ | Bulgaria
  • USD $ | Cambodia
  • USD $ | Canada
  • USD $ | Chile
  • USD $ | China
  • USD $ | Colombia
  • USD $ | Costa Rica
  • USD $ | Croatia
  • USD $ | Cyprus
  • USD $ | Czechia
  • USD $ | Denmark
  • USD $ | Estonia
  • USD $ | Finland
  • USD $ | France
  • USD $ | Georgia
  • USD $ | Germany
  • USD $ | Greece
  • USD $ | Hong Kong SAR
  • USD $ | Hungary
  • USD $ | Iceland
  • USD $ | India
  • USD $ | Ireland
  • USD $ | Israel
  • USD $ | Italy
  • USD $ | Japan
  • USD $ | Kazakhstan
  • USD $ | Latvia
  • USD $ | Liechtenstein
  • USD $ | Lithuania
  • USD $ | Madagascar
  • USD $ | Malta
  • USD $ | Mexico
  • USD $ | Moldova
  • USD $ | Monaco
  • USD $ | Netherlands
  • USD $ | New Zealand
  • USD $ | North Macedonia
  • USD $ | Norway
  • USD $ | Panama
  • USD $ | Paraguay
  • USD $ | Peru
  • USD $ | Philippines
  • USD $ | Poland
  • USD $ | Portugal
  • USD $ | Romania
  • USD $ | Singapore
  • USD $ | Slovakia
  • USD $ | Slovenia
  • USD $ | South Africa
  • USD $ | South Korea
  • USD $ | Spain
  • USD $ | Sri Lanka
  • USD $ | Sweden
  • USD $ | Switzerland
  • USD $ | Taiwan
  • USD $ | Thailand
  • USD $ | Türkiye
  • USD $ | Ukraine
  • USD $ | United Kingdom
  • USD $ | United States
  • USD $ | Uruguay
  • USD $ | Vatican City
  • USD $ | Venezuela
  • USD $ | Vietnam
  • Facebook
  • Instagram
logoProSpec - Recombinant Protein Manufacturer for academic and R&D industry
Become a distributor
Account Log in
Wishlist
Cart Cart(0)
  • Products
    +
    • Cytokines
    • Growth factors
    • Chemokines
    • Cd antigens
    • Neurotrophins
    • Hormones
    • Enzymes
    • Viral antigens
    • Recombinant proteins
    • Natural proteins
    • Monoclonal antibodies
    • Polyclonal antibodies
    • Thermal Packaging
  • About
    +
    • Company
    • Founder
    • Contribution
  • Customers
    +
    • Eastern Asia
    • Eastern Europe
    • North America
    • South America
    • South East Asia
    • Southern Asia
    • Western Europe
  • Ordering
    +
    • Ordering Method
    • Ordering - Credit Card
    • Ordering - PO
    • Shipping Fees
    • FAQs
  • Services
    +
    • DNA Cloning
    • Protein Expression
    • Monoclonal Antibody
    • Fermentation
    • Technology License
  • Contact us

Item added to your cart

View cart
View All
  • 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

    View All
  • 4-1BB

    4-1BB

    View All
  • Adiponectin

    Adiponectin

    View All
  • AIF1

    AIF1

    View All
  • Other Cytokines

    Other Cytokines

    View All
  • AITRL

    AITRL

    View All
  • Angiopoietin

    Angiopoietin

    View All
  • Apolipoprotein

    Apolipoprotein

    View All
  • B-Cell Activating Factor

    B-Cell Activating Factor

    View All
  • Beta Defensin

    Beta Defensin

    View All
  • Bone Morphogenetic Protein

    Bone Morphogenetic Protein

    View All
  • B type Natriuretic Peptide

    B type Natriuretic Peptide

    View All
  • BST

    BST

    View All
  • Betacellulin

    Betacellulin

    View All
  • Cardiotrophin

    Cardiotrophin

    View All
  • Activin

    Activin

    View All
  • Fibroblast Growth Factor

    Fibroblast Growth Factor

    View All
  • Other Growth Factors

    Other Growth Factors

    View All
  • CSF

    CSF

    View All
  • CTGF

    CTGF

    View All
  • IGFBP

    IGFBP

    View All
  • VEGF Protein

    VEGF Protein

    View All
  • EGF

    EGF

    View All
  • Epigen

    Epigen

    View All
  • Erythropoietin

    Erythropoietin

    View All
  • Insulin-Like Growth Factor

    Insulin-Like Growth Factor

    View All
  • Growth Hormone

    Growth Hormone

    View All
  • HDGF

    HDGF

    View All
  • Hepatocyte Growth Factor

    Hepatocyte Growth Factor

    View All
  • Insulin

    Insulin

    View All
  • BCA-1/ BLC (CXCL13)

    BCA-1/ BLC (CXCL13)

    View All
  • BRAK (CXCL14)

    BRAK (CXCL14)

    View All
  • C-10 (CCL6)

    C-10 (CCL6)

    View All
  • Other Chemokines

    Other Chemokines

    View All
  • MEC (CCL28)

    MEC (CCL28)

    View All
  • LD78-beta (CCL3L1)

    LD78-beta (CCL3L1)

    View All
  • CTACK (CCL27)

    CTACK (CCL27)

    View All
  • CXCL16

    CXCL16

    View All
  • CXCL17

    CXCL17

    View All
  • Platelet Factor-4 (CXCL4)

    Platelet Factor-4 (CXCL4)

    View All
  • ENA-78 (CXCL5)

    ENA-78 (CXCL5)

    View All
  • Eotaxin (CCL11,24,26)

    Eotaxin (CCL11,24,26)

    View All
  • Exodus-2 (CCL21)

    Exodus-2 (CCL21)

    View All
  • Fractalkine (CX3CL1)

    Fractalkine (CX3CL1)

    View All
  • CXCL6

    CXCL6

    View All
  • Other CD Antigens

    Other CD Antigens

    View All
  • CD14

    CD14

    View All
  • CD164

    CD164

    View All
  • CD1

    CD1

    View All
  • CD2

    CD2

    View All
  • CD200

    CD200

    View All
  • CD207

    CD207

    View All
  • CD226

    CD226

    View All
  • CD23

    CD23

    View All
  • CD244

    CD244

    View All
  • CD247

    CD247

    View All
  • CD27

    CD27

    View All
  • CD274

    CD274

    View All
  • CD300

    CD300

    View All
  • CD33

    CD33

    View All
  • Other Neurotrophins

    Other Neurotrophins

    View All
  • Beta-NGF

    Beta-NGF

    View All
  • BDNF

    BDNF

    View All
  • CDNF

    CDNF

    View All
  • CNTF

    CNTF

    View All
  • GDNF

    GDNF

    View All
  • Glia Maturation Factor

    Glia Maturation Factor

    View All
  • MANF

    MANF

    View All
  • Midkine

    Midkine

    View All
  • Neuroglobin

    Neuroglobin

    View All
  • Neurotrophic factors

    Neurotrophic factors

    View All
  • Neuregulin

    Neuregulin

    View All
  • Neuropilin

    Neuropilin

    View All
  • Pigment Epithelium-Derived Factor

    Pigment Epithelium-Derived Factor

    View All
  • Pleiotrophin

    Pleiotrophin

    View All
  • Peptide Hormones

    Peptide Hormones

    View All
  • Other Hormones

    Other Hormones

    View All
  • HCG

    HCG

    View All
  • Endothelin

    Endothelin

    View All
  • Exendin

    Exendin

    View All
  • FSH

    FSH

    View All
  • Glucagon

    Glucagon

    View All
  • GHRP

    GHRP

    View All
  • GLP

    GLP

    View All
  • Thyrostimulin

    Thyrostimulin

    View All
  • Inhibin A

    Inhibin A

    View All
  • LHRH

    LHRH

    View All
  • Melanotan

    Melanotan

    View All
  • Procalcitonin

    Procalcitonin

    View All
  • PTH

    PTH

    View All
  • Peroxiredoxin

    Peroxiredoxin

    View All
  • Peptidase

    Peptidase

    View All
  • Synthetase

    Synthetase

    View All
  • Transferase

    Transferase

    View All
  • Hydrolase

    Hydrolase

    View All
  • Dehydrogenase

    Dehydrogenase

    View All
  • ACE2

    ACE2

    View All
  • Esterase

    Esterase

    View All
  • Protein Kinases

    Protein Kinases

    View All
  • Other Enzymes

    Other Enzymes

    View All
  • Phosphatase

    Phosphatase

    View All
  • Deaminase

    Deaminase

    View All
  • Oxygenase

    Oxygenase

    View All
  • Adenylate Kinase

    Adenylate Kinase

    View All
  • Lyase

    Lyase

    View All
  • Chagas

    Chagas

    View All
  • SARS

    SARS

    View All
  • Influenza

    Influenza

    View All
  • ASFV

    ASFV

    View All
  • Astrovirus

    Astrovirus

    View All
  • Borrelia

    Borrelia

    View All
  • Helicobacter Pylori

    Helicobacter Pylori

    View All
  • Chikungunya

    Chikungunya

    View All
  • Chlamydia

    Chlamydia

    View All
  • Cytomegalo

    Cytomegalo

    View All
  • Dengue

    Dengue

    View All
  • EBV

    EBV

    View All
  • Ebola

    Ebola

    View All
  • Feline Leukemia Virus

    Feline Leukemia Virus

    View All
  • Hepatitis A

    Hepatitis A

    View All
  • Other

    Other

    View All
  • Actin

    Actin

    View All
  • ADAM

    ADAM

    View All
  • Complement Component

    Complement Component

    View All
  • Ag85

    Ag85

    View All
  • Eukaryotic Translation Initiation Factor

    Eukaryotic Translation Initiation Factor

    View All
  • Anterior Gradient Protein

    Anterior Gradient Protein

    View All
  • Heat Shock Protein

    Heat Shock Protein

    View All
  • Alpha-2-HS-Glycoprotein

    Alpha-2-HS-Glycoprotein

    View All
  • Hemoglobin

    Hemoglobin

    View All
  • Allergy

    Allergy

    View All
  • Anaplasma

    Anaplasma

    View All
  • Angiogenin

    Angiogenin

    View All
  • Ankyrin Repeat Domain

    Ankyrin Repeat Domain

    View All
  • Annexin

    Annexin

    View All
  • Other Natural Proteins

    Other Natural Proteins

    View All
  • Aprotinin

    Aprotinin

    View All
  • Transferrin

    Transferrin

    View All
  • Avidin

    Avidin

    View All
  • Anti Coagulation Factors

    Anti Coagulation Factors

    View All
  • Natural Albumin

    Natural Albumin

    View All
  • Natural Coagulation Factors

    Natural Coagulation Factors

    View All
  • Fibronectin

    Fibronectin

    View All
  • Thrombin

    Thrombin

    View All
  • Anti Human Enzyme

    Anti Human Enzyme

    View All
  • Other Monoclonal Antibodies

    Other Monoclonal Antibodies

    View All
  • Anti Human Cytokine

    Anti Human Cytokine

    View All
  • Anti Human Heat Shock Protein

    Anti Human Heat Shock Protein

    View All
  • Anti Mouse Lymphocyte

    Anti Mouse Lymphocyte

    View All
  • Anti Human Chemokine

    Anti Human Chemokine

    View All
  • Anti Human Lymphocyte

    Anti Human Lymphocyte

    View All
  • Anti Viral Monoclonal

    Anti Viral Monoclonal

    View All
  • Anti Mouse Cytokine

    Anti Mouse Cytokine

    View All
  • Anti-GST Monoclonal

    Anti-GST Monoclonal

    View All
  • Other Polyclonal Antibodies

    Other Polyclonal Antibodies

    View All
  • Anti Viral

    Anti Viral

    View All
  • Anti-GST Monoclonal

    Anti-GST Monoclonal

    View All
Back

Search results

1000 results found for “CNTF”

Name

Description

Product #

Price

Quantity

Shipping Method

  • View Data Sheet

    Name :

    NT-proBNP Human

    Description:

    NT-Pro-B-type Natriuretic Protein Human Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-1118

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • sds-page

    Description

    NT-Pro-B-type Natriuretic Protein Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 76 amino acid and having a molecular mass of approximately 8.5kDa. NT-proBNP 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 and 150mM NaCl.

    Purity

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

    sds-page

    NT-ProBNP sds-page - Product image 1

    More Info

    • Introduction

      Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis,vasorelaxation,diuresis and inhibition of renin and aldosterone secretion. BNP plays a key role in cardiovascular homeostasis. BNP also helps restore the body's salt and water balance andimproves heart function.

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HPLGSPGSAS DLETSGLQEQ RNHLQGKLSE LQVEQTSLEP LQESPRPTGV WKSREVATEG IRGHRKMVLY TLRAPR.

    • Background

      What is the molecular weight / Mw of NT-proBNP?
      NT-proBNP has a total Mw of 8.5kDa.

      What is the source or expression system of NT-proBNP?
      Escherichia Coli.

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

      What is the Biological Activity of NT-proBNP?
      The biological functionality of NT-proBNP will be determined in the future.

      What is the amino acid sequence of NT-proBNP?
      HPLGSPGSAS DLETSGLQEQ RNHLQGKLSE LQVEQTSLEP LQESPRPTGV WKSREVATEG IRGHRKMVLY TLRAPR.

      What applications can NT-proBNP be used in?
      NT-proBNP can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for NT-proBNP?
      The endotoxin level is minimal, NT-proBNP 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.

    Nt Probnp Human
  • View Data Sheet

    Name :

    M CSF Human, His

    Description:

    Macrophage Colony Stimulating Factor Human Recombinant, His Tag

    CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-695

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 179 amino acids (33-190 a.a.) and having a total molecular mass of 20.7 kDa.MCSF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MCSF protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT & 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    • 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 MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ DVVTKPDCN.

    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.

    M Csf Human His
  • View Data Sheet

    Name :

    OTC Human

    Description:

    Ornithine Carbamoyltransferase Human Recombinant

    Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.

    Product # :

    ENZ-596

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    OTC Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (33-354) and having a molecular mass of 38.9kDa.OTC is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The OTC solution (0.5mg/ml) contains 20mM MES buffer (pH 6.0), 100mM Nacl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.

    • Synonyms

      Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.

    • 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 MGSHMNKVQL KGRDLLTLKN FTGEEIKYML WLSADLKFRI KQKGEYLPLL QGKSLGMIFE KRSTRTRLST ETGFALLGGH PCFLTTQDIH LGVNESLTDT ARVLSSMADA VLARVYKQSD LDTLAKEASI PIINGLSDLY HPIQILADYL TLQEHYSSLK GLTLSWIGDG NNILHSIMMS AAKFGMHLQA ATPKGYEPDA SVTKLAEQYA KENGTKLLLT NDPLEAAHGG NVLITDTWIS MGQEEEKKKR LQAFQGYQVT MKTAKVAASD WTFLHCLPRK PEEVDDEVFY SPRSLVFPEA ENRKWTIMAV MVSLLTDYSP QLQKPKF.

    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.

    Otc Human
  • View Data Sheet

    Name :

    CD116 Human

    Description:

    GM-CSF Receptor Alpha Human Recombinant

    CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

    Product # :

    CYT-796

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • sds-page

    Description

    CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (20-320 a.a) and having a molecular mass of 37.2kDa.CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSF2RA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    CD116 Human-sds-page - Product image 1

    More Info

    • Introduction

      GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.

    • Synonyms

      CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

    • 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.

    • Background

      Unlocking the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Implications and Applications

      Abstract:

      The Ciliary Neurotrophic Factor Receptor (CNTFR) plays a pivotal role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper examines the significance of Human Recombinant CNTFR, its production techniques, and its potential applications in neurobiology and therapeutic interventions. The review underscores CNTFR's crucial role in advancing neuroprotection and neuroregeneration research.

      Introduction:

      CNTFR, a transmembrane protein, is central to transducing the signals initiated by CNTF. Availability of Human Recombinant CNTFR enables researchers to dissect its contribution to neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's role in modulating neuronal health and promoting regeneration makes it a cornerstone in neurobiology.

      Role in CNTF Signaling:

      CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and trigger downstream signaling pathways. Activation of intracellular cascades, such as JAK/STAT and MAPK, is instrumental in driving the neuroprotective and growth-promoting effects of CNTF.

      Production Methods:

      Human Recombinant CNTFR is generated through gene expression in suitable host cells, often utilizing bacterial or mammalian systems. Ensuring accurate folding and post-translational modifications is crucial to preserve its functionality and affinity for CNTF.

      Therapeutic Applications:

      Human Recombinant CNTFR holds promise for therapeutic applications in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-associated signaling presents opportunities to bolster neuronal survival and regeneration, potentially revolutionizing patient care.

      Challenges and Future Directions:

      While the potential is significant, challenges encompass optimizing CNTFR-CNTF interactions, effective tissue delivery, and understanding potential off-target effects. Ongoing research is paramount to unravel the complete mechanisms of CNTFR-mediated signaling and its therapeutic implications.

      Conclusion:

      Human Recombinant Ciliary Neurotrophic Factor Receptor emerges as a vital tool in advancing our grasp of neuroprotection and regeneration. Its capacity to modulate CNTF effects opens doors to innovative therapeutic strategies for addressing neurodegenerative disorders, embodying the intersection of molecular insights and clinical progress.

      What is the molecular weight/Mw of CD116 Protein?
      CD116 Protein has a total Mw of 37.2kDa.

      What is the source or expression system of CD116 Protein?
      Escherichia Coli.

      What is the Purity of CD116 Protein?
      CD116 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD116 Protein?
      The biological functionality of CD116 Protein will be determined in the future.

      What is the amino acid sequence of CD116 Protein?
      CD116 Protein is composed from 324 amino acids.

      What applications can CD116 Protein be used in?
      CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD116 Protein?
      The endotoxin level is minimal, CD116 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.

    Csf2Ra Human
  • View Data Sheet

    Name :

    MTPN Human

    Description:

    Myotrophin Human Recombinant

    Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.

    Product # :

    CYT-723

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    MTPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 15 kDa. The MTPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MTPN Human solution containing 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MTPN is an ankyrin repeat protein, that stimulates protein synthesis and cardiomyocyte growth to commence cardiac hypertrophy by activating the NF-kappaB signaling cascade. Myotrophin participates in cerebellar morphogenesis and takes part in differentiation of cerebellar neurons, particularly of granule cells. High levels of MTPN are expressed in human dilated cardiomyopathic and ischemic hearts.

    • Synonyms

      Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.

    • 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 MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ.

    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.

    Mtpn Human
  • View Data Sheet

    Name :

    BDNF Human, His

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant, His Tag

    Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

    Product # :

    CYT-881

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • sds-page

    Description

    BDNF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (129-247 a.a) and having a molecular mass of 15.8kDa. BDNF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BDNF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    BDNF-sds-page - Product image 1

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

    • 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 MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 15.8kDa.

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

      What is the Purity of BDNF Protein?
      BDNF Protein is >85% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of BDNF Protein?
      MGSSHHHHHH SSGLVPRGSH MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    Bdnf Human His
  • View Data Sheet

    Name :

    C17ORF103 Human

    Description:

    Chromosome 17 Open Reading Frame 103 Human Recombinant

    Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.

    Product # :

    PRO-1619

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    C17ORF103 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113) and having a molecular mass of 15.4kDa.C17ORF103 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C17ORF103 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      C17orf103 is a member of the GTLF3B family and is encoded by a gene which is located in human chromosome 17p11.2. BRCA1 and p53 are 2 main tumor suppressor genes which are linked to chromosome 17. Tumor suppressor p53 is necessary for maintenance of cellular genetic integrity by moderating cell fate through DNA repair versus cell death. C17orf103 is also related to neurofibromatosis, a disorder characterized by neural and epidermal lesions, and dysregulated Schwann cell growth.

    • Synonyms

      Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.

    • 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 MGSMAHSAAA VPLGALEQGC PIRVEHDRRR RQFTVRLNGC HDRAVLLYEY VGKRIVDLQH TEVPDAYRGR GIAKHLAKAA LDFVVEEDLK AHLTCWYIQK YVKENPLPQY LERLQP

    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.

    C17Orf103 Human
  • View Data Sheet

    Name :

    TFF2 Human

    Description:

    Trefoil Factor-2 Human Recombinant

    TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    Product # :

    CYT-612

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 106 amino acids (24-129) and having a total molecular mass of 12 kDa. TFF2 Human Recombinant includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds and was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 1mg/mL containing 1x PBS pH-7.4.

    Purity

    Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human MCF-7 cells using a concentration 1.0-10.0 ng/ml.

    More Info

    • Introduction

      Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.

    • Synonyms

      TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 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 TFF2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.

    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.

    Tff2 Human
  • View Data Sheet

    Name :

    OPG Fc Human

    Description:

    Osteoprotegerin Human Recombinant /Fc Chimera

    TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    Product # :

    CYT-266

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Recombinant OPG produced in yeast contains 2x412 amino acid residues, including 180 residues from mature OPG (a.a 22-201) and 232 residues from the Fc protein of human IgG1, and has a calculated molecular mass of 109.6kDa.

    Source

    Pichia Pastoris.

    Formulation

    OPG was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 6.0, 150mM NaCl and 0.02 % Tween-80.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by neutralizing the stimulation of U937 cells is less tha10ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg in the presence of 10ng/ml soluble Human RANKL (sRANKL).

    More Info

    • Introduction

      Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

    • Synonyms

      TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      OPG 22-201 ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQKCGIDVTL
      Fc232EPKSSDKTHT CPPCPAPEFE GAPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPTPIEKTISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK

    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.

    Osteoprotegerin Human
  • View Data Sheet

    Name :

    CST3 Mouse

    Description:

    Cystatin-C Mouse Recombinant

    Post G-globulin, CST 3, CST3, Gamma-Trace, Cystatin 3, Amyloid Angiopathy and Cerebral Hemorrhage, Cystatin-C precursor, neuroendocrine basic polypeptide.

    Product # :

    PRO-597

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Cystatin-C Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15kDa. The Mouse Cystatin-C is fused to His tag at N-Terminus.The Mouse Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Post G-globulin, CST 3, CST3, Gamma-Trace, Cystatin 3, Amyloid Angiopathy and Cerebral Hemorrhage, Cystatin-C precursor, neuroendocrine basic polypeptide.

    • Physical Appearance

      Sterile 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.

    • Solubility

      Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MRGSHHHHHH GMASATPKQG PRMLGAPEEA DANEEGVRRA LDFAVSEYNK GSNDAYHSRA IQVVRARKQL VAGVNYFLDV EMGRTTCTKS QTNLTDCPFH DQPHLMRKAL CSFQIYSVPW KGTHSLTKFSCKNA.

    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.

    Cystatin C Mouse
  • View Data Sheet

    Name :

    CST3 Rat, sf9

    Description:

    Cystatin C Rat Recombinant, sf9

    Cystatin-C, Cystatin-3.

    Product # :

    PRO-2311

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CST3 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 128 amino acids (21-140a.a.) and having a molecular mass of 14.3kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). CST3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques

    Source

    Sf9, Baculovirus cells.

    Formulation

    CST3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3.

    • 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

      GTSRPPPRLL GAPQEADASE EGVQRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGI NYYLDVEMGR TTCTKSQTNL TNCPFHDQPH LMRKALCSFQ IYSVPWKGTH TLTKSSCKNA 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.

    Cst3 Rat Sf9
  • View Data Sheet

    Name :

    TAF10 Human

    Description:

    TAF10 RNA Polymerase II Human Recombinant

    TAF10 RNA Polymerase II TATA Box Binding Protein (TBP)-Associated Factor 30kDa, Transcription Initiation Factor TFIID 30 KDa Subunit, STAF28, TAF2A, TAF2H.

    Product # :

    ENZ-750

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TAF10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (84-218) and having a molecular mass of 16.9kDa.TAF10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TAF10 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TAF10 is a small subunit of TFIID which is related to a subdivision of TFIID complexes. Studies with human and mammalian cells verified that this subunit is mandatory for transcriptional activation by the estrogen receptor, for progression through the cell cycle, and is essential for several cellular differentiation programs.

    • Synonyms

      TAF10 RNA Polymerase II TATA Box Binding Protein (TBP)-Associated Factor 30kDa, Transcription Initiation Factor TFIID 30 KDa Subunit, STAF28, TAF2A, TAF2H.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSGAAPPEG AISNGVYVLP SAANGDVKPV VSSTPLVDFL MQLEDYTPTI PDAVTGYYLN RAGFEASDPR IIRLISLAAQ KFISDIANDA LQHCKMKGTA SGSSRSKSKD RKYTLTMEDL TPALSEYGIN VKKPHYFT

    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.

    Taf10 Human
  • View Data Sheet

    Name :

    G CSF Human, HEK

    Description:

    Granulocyte-Colony Stimulating Factor Human Recombinant, HEK

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-088

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    G-CSF Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 21-25kDa due to glycosylation.The G-CSF is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The G-CSF was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells (Mouse Myeloid Leukemia indicator cell line), the ED50 is <0.01ng/ml.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution G-CSF 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 G-CSF in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.

    • Background

      What is the molecular weight/Mw of G CSF HUMAN, HEK Protein?
      G CSF HUMAN, HEK Protein has a total Mw of 23kDa.

      What is the source or expression system of G CSF HUMAN, HEK Protein?
      HEK.

      What is the Purity of G CSF HUMAN, HEK Protein?
      G CSF HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of G CSF HUMAN, HEK Protein?
      The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells (Mouse Myeloid Leukemia indicator cell line), the ED50 is <0.01ng/ml.

      What applications can G CSF HUMAN, HEK Protein be used in?
      G CSF HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for G CSF HUMAN, HEK Protein?
      The endotoxin level is minimal, G CSF 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.

    G Csf Human Hek
  • View Data Sheet

    Name :

    VEGF Human, Yeast

    Description:

    Vascular Endothelial Growth Factor Human Recombinant, Yeast

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-577

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    Vascular Endothelial Growth Factor Human Recombinant produced in Yeast is a double, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 42 kDa.

    Source

    Pichia Pastoris.

    Formulation

    The protein contains 20mM Phosphate- Buffered Saline, pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its ability to stimulate 3H-Thymidine incorporation in human umbilical vein endothelial cells, the ED50 for this effect was found to be 2-6ng/ml.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      Vascular Endothelial Growth Factor Human although stable at 15°C for 2 weeks, should be stored 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.

    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.

    Vegf Human Yeast
  • View Data Sheet

    Name :

    SCF Rat

    Description:

    Stem Cell Factor Rat Recombinant

    Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.

    Product # :

    CYT-323

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Stem cell factor Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (26-189) and having a molecular mass of 18.4 kDa.The Rat SCF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

    Purity

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

    Biological Activity

    The ED50 is determined by the dose-dependant stimulation of the proliferation of human TF-1 cells which is < 10 ng/ml, corresponding to a specific activity of 100,000units/mg.

    More Info

    • Introduction

      Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117 (c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
      SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).

    • Synonyms

      Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MQEICRNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV THLSVSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVAC MEENAPKNVK ESLKKPETRN FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.

    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.

    Scf Rat
  • View Data Sheet

    Name :

    EGF Mouse, Biotin

    Description:

    Epidermal Growth Factor Mouse Recombinant, Biotin

    Urogastrone, URG, EGF.

    Product # :

    CYT-841

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.

    Source

    Escherichia Coli.

    Formulation

    The protein (0.5mg/ml) solution contains sterile PBS.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Should be stored at 4°C.Please do not freeze.

    • Amino Acid Sequence

      MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

    • Background

      Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential

      Abstract:

      This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.

      Introduction:

      Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.

      Protein Engineering and Biotin Conjugation:

      EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.

      Cellular Signaling Amplification:

      The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.

      Cellular Assays and Functional Responses:

      In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.

      Tailored Delivery Strategies:

      The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.

      Regenerative Medicine and Targeted Therapy:

      The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.

      Future Prospects and Challenges:

      While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.

      Conclusion:

      In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.

      What is the molecular weight/Mw of MEGF, BIOTIN Protein?
      MEGF, BIOTIN Protein has a total Mw of 7kDa.

      What is the source or expression system of MEGF, BIOTIN Protein?
      Escherichia Coli.

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

      What is the Biological Activity of MEGF, BIOTIN Protein?
      The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

      What is the amino acid sequence of MEGF, BIOTIN Protein?
      MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

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

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

    Egf Mouse Biotin
  • View Data Sheet

    Name :

    FLT1 Human

    Description:

    Vascular Endothelial Growth Factor Receptor-1 Human Recombinant

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-240

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity of FLT1 was determined by its ability to inhibit the VEGF (165)-induced proliferation of HUVECs.

    More Info

    • Introduction

      Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH

    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.

    Flt1 Human
  • View Data Sheet

    Name :

    EGFR Human, CHO

    Description:

    Epidermal Growth Factor Receptor, CHO Human Recombinant

    Epidermal Growth Factor Receptor, Receptor Tyrosine-Protein Kinase ErbB-1, Erb-B2 Receptor Tyrosine Kinase, Proto-Oncogene C-ErbB-1, EC 2.7.10.1, ERBB1, ERBB, HER1, Epidermal Growth Factor Receptor (Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog), Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog (Avian), Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog, Cell Proliferation-Inducing Protein 61, Cell Growth Inhibiting Protein 40, EC 2.7.10, NISBD2, PIG61, MENA.

    Product # :

    PKA-086

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EGFR produced in CHO cells is a single, glycosylated polypeptide chain containing 860 amino acids (25-645 a.a.) and having a molecular mass of 95.5 kDa (Migrates at 100-150 on SDS-PAGE under reducing conditions). EGFR is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary cells.

    Formulation

    EGFR 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.

    More Info

    • Introduction

      The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGFa , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

    • Synonyms

      Epidermal Growth Factor Receptor, Receptor Tyrosine-Protein Kinase ErbB-1, Erb-B2 Receptor Tyrosine Kinase, Proto-Oncogene C-ErbB-1, EC 2.7.10.1, ERBB1, ERBB, HER1, Epidermal Growth Factor Receptor (Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog), Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog (Avian), Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog, Cell Proliferation-Inducing Protein 61, Cell Growth Inhibiting Protein 40, EC 2.7.10, NISBD2, PIG61, MENA.

    • 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

      LEEKKVCQGT SNKLTQLGTF EDHFLSLQRM FNNCEVVLGN LEITYVQRNY DLSFLKTIQE VAGYVLIALN TVERIPLENL QIIRGNMYYE NSYALAVLSN YDANKTGLKE LPMRNLQEIL HGAVRFSNNP ALCNVESIQW RDIVSSDFLS NMSMDFQNHL GSCQKCDPSC PNGSCWGAGE ENCQKLTKII CAQQCSGRCR GKSPSDCCHN QCAAGCTGPR ESDCLVCRKF RDEATCKDTC PPLMLYNPTT YQMDVNPEGK YSFGATCVKK CPRNYVVTDH GSCVRACGAD SYEMEEDGVR KCKKCEGPCR KVCNGIGIGE FKDSLSINAT NIKHFKNCTS ISGDLHILPV AFRGDSFTHT PPLDPQELDI LKTVKEITGF LLIQAWPENR TDLHAFENLE IIRGRTKQHG QFSLAVVSLN ITSLGLRSLK EISDGDVIIS GNKNLCYANT INWKKLFGTS GQKTKIISNR GENSCKATGQ VCHALCSPEG CWGPEPRDCV SCRNVSRGRE CVDKCNLLEG EPREFVENSE CIQCHPECLP QAMNITCTGR GPDNCIQCAH YIDGPHCVKT CPAGVMGENN TLVWKYADAG HVCHLCHPNC TYGCTGPGLE GCPTNGPKIP SRSPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.

    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.

    Egfr Human Cho
  • View Data Sheet

    Name :

    RANK Human

    Description:

    RANK Human Recombinant

    TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265

    Product # :

    CYT-734

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    RANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of 19.1kDa. The RANK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH 8.0 and 150mM 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 its ability to inhibit sRANK Ligand induced nuclear factor kappa B (NFkappaB) in RAW 264.7 cells is less than 50 ng/ml, corresponding to a specific activity of
    > 2.0 × 104 IU/mg in the presence of 15 ng/ml of recombinant sRANK Ligand.

    More Info

    • Introduction

      sRANK Receptor is a part of of the TNF superfamily of ligands and receptors which participates in the regulation of specific immunity and bone turnover. sRANK Receptor was originally acknowledged as a dendritic-cell-membrane protein, which by interacting with RANKL augments the capacity of dendritic cells to stimulate naive T cell proliferation and to endorse the survival of RANK and T cells. The full length human RANK cDNA encodes a type I transmembrane protein of 616 amino acids with a predicted 183 amino acid extracellular domain and a 383 amino acid cytoplasmic domain. sRANK Receptor is also expressed in a various tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.

    • Synonyms

      TNFRSF11A, ODFR, RANK, Tumor Necrosis Factor Receptor Superfamily, Member 11a, Activator Of NFKB, Receptor Activator Of Nuclear Factor-Kappa B, CD265 Antigen, LOH18CR1, TRANCER, CD265

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QIAPPCTSEK HYEHLGRCCN KCEPGKYMSS KCTTTSDSVC LPCGPDEYLD SWNEEDKCLL HKVCDTGKAL VAVVAGNSTT PRRCACTAGY HWSQDCECCR RNTECAPGLG AQHPLQLNKD TVCKPCLAGY FSDAFSSTDK CRPWTNCTFL GKRVEHHGTE KSDAVCSSSL PARK.

    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.

    Tnfrsf11A Human
  • View Data Sheet

    Name :

    CST4 Human, sf9

    Description:

    Cystatin 4 Human Recombinant, sf9

    Cystatin S, Salivary Acidic Protein 1, Cystatin-SA-III, Cystatin-4, Cystatin 4, Cystatin-S.

    Product # :

    PRO-2250

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CST4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 131 amino acids (21-141 a.a.) and having a molecular mass of 15.4kDa (Migrates at 13.5-18kDa on SDS-PAGE under reducing conditions). CST4 is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CST4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CST4 is a member of the cystatin superfamily which contains proteins that hold multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, whereas others have lost or possibly never attained this inhibitory activity. CST4 strongly inhibits papain (non-competitively) and ficin, partially inhibits stem bromelain and bovine cathepsin C, however does not inhibit porcine cathepsin B or clostripain.

    • Synonyms

      Cystatin S, Salivary Acidic Protein 1, Cystatin-SA-III, Cystatin-4, Cystatin 4, Cystatin-S.

    • 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

      ADPMSSSKEE NRIIPGGIYD ADLNDEWVQR ALHFAISEYN KATEDEYYRR PLQVLRAREQ TFGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WEDRMSLVNS RCQEAHHHHH H.

    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.

    Cst4 Human Sf9
  • View Data Sheet

    Name :

    CTHRC1 Human, Sf9

    Description:

    Collagen Triple Helix Repeat Containing 1 Human Recombinant, Sf9

    Collagen triple helix repeat-containing protein 1 isoform 1, CTHRC1, Protein NMTC1.

    Product # :

    PRO-2606

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CTHRC1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 222 amino acids (31-243a.a.) and having a molecular mass of 24.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTHRC1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTHRC1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Collagen triple helix repeat-containing protein 1 or CTHRC1 acts as a negative regulator of collagen matrix deposition. The protein is secreted from a 28kDa protein which is glycosylated and very conserved from lower chordates to mammals. CTHRC1 is found qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers.CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells.

    • Synonyms

      Collagen triple helix repeat-containing protein 1 isoform 1, CTHRC1, Protein NMTC1.

    • 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

      ADPSEIPKGK QKAQLRQREV VDLYNGMCLQ GPAGVPGRDG SPGANGIPGT PGIPGRDGFK GEKGECLRES FEESWTPNYK QCSWSSLNYG IDLGKIAECT FTKMRSNSAL RVLFSGSLRL KCRNACCQRW YFTFNGAECS GPLPIEAIIY LDQGSPEMNS TINIHRTSSV EGLCEGIGAG LVDVAIWVGT CSDYPKGDAS TGWNSVSRII IEELPKHHHH HH.

    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.

    Cthrc1 Protein
  • View Data Sheet

    Name :

    NOV Human, HEK

    Description:

    Nephroblastoma Overexpressed Human Recombinant, HEK

    Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    Product # :

    CYT-1032

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 33-357) containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    NOV filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

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

    • Amino Acid Sequence

      QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEVSDS SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.

    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.

    Nov Protein
  • View Data Sheet

    Name :

    EIF4E Human

    Description:

    Eukaryotic Translation Initiation Factor 4E Human Recombinant

    CBP, EIF4E1, EIF4EL1, EIF4F.

    Product # :

    PRO-530

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EIF4E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular weight of 27.2kDa. The EIF4E is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF4E 0.5mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.

    • Synonyms

      CBP, EIF4E1, EIF4EL1, EIF4F.

    • 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 MATVEPETTP TPNPPTTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL RLISKFDTVE
      DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG
      DKIAIWTTEC ENREAVTHIG RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV.

    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.

    Eif4E Human
  • View Data Sheet

    Name :

    GNPNAT1 Human

    Description:

    Glucosamine-Phosphate N-Acetyltransferase 1 Human Recombinant

    Gpnat1, GNPNAT, GNA1, EC 2.3.1.4, FLJ10607, Glucosamine-Phosphate N-Acetyltransferase 1, Phosphoglucosamine acetylase, Phosphoglucosamine transacetylase, Glucosamine 6-Phosphate N-Acetyltransferase.

    Product # :

    ENZ-037

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    GNPNAT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-184a.a.) and having a molecular mass of 23.1KDa.GNPNAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GNPNAT1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNPNAT1 is a member of the GNA1 subfamily of the larger acetyltransferase family of proteins. GNPNAT1 is limited to the Golgi apparatus and the endosome. GNPNAT1 is vital for UDPGlcNAc biosynthesis pathway. GNPNAT1 catalyzes the synthesis of GlcNAc6P from AcCoA and GlcN6P, a step in the UDP-GlcNAc6P formation pathway.

    • Synonyms

      Gpnat1, GNPNAT, GNA1, EC 2.3.1.4, FLJ10607, Glucosamine-Phosphate N-Acetyltransferase 1, Phosphoglucosamine acetylase, Phosphoglucosamine transacetylase, Glucosamine 6-Phosphate N-Acetyltransferase.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMKPDETP MFDPSLLKEV DWSQNTATFS PAISPTHPGE GLVLRPLCTA DLNRGFFKVL GQLTETGVVS PEQFMKSFEH MKKSGDYYVT VVEDVTLGQI VATATLIIEH KFIHSCAKRG RVEDVVVSDE CRGKQLGKLL LSTLTLLSKK LNCYKITLEC
      LPQNVGFYKK FGYTVSEENY MCRRFLK

    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.

    Gnpnat1 Human
  • 1
  • …
  • 11
  • 12
  • 13
  • 14
  • 15
  • …
  • 42
Your browser does not support the video tag.

Products

  • Cytokines
  • Growth Factors
  • Chemokines
  • CD Antigens
  • Neurotrophins
  • Hormones
  • Enzymes
  • Viral Antigens
  • Recombinant Proteins
  • Natural Proteins
  • Monoclonal Antibodies
  • Polyclonal Antibodies
  • Thermal Packaging

About

  • Company
  • Founder
  • Contribution
  • Contact Us
  • My Account

Ordering

  • Ordering Method
  • Ordering - Credit Card
  • Ordering PO
  • Shipping Fees
  • FAQ's

Legal

  • Terms & Conditions
  • Privacy
  • Site Map
  • info@prospecbio.com
  • Facebook
  • Instagram
  • Linkedin Profile

© 2026 ProSpec-Tany TechnoGene Ltd. All Rights Reserved.

  • Choosing a selection results in a full page refresh.
  • Opens in a new window.