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 “stathmin”

Name

Description

Product #

Price

Quantity

Shipping Method

  • View Data Sheet

    Name :

    LECT2 Human

    Description:

    Leukocyte Cell-Derived Chemotaxin 2 Human Recombinant

    Leukocyte Cell-Derived Chemotaxin 2, Leukocyte Cell-Derived Chemotaxin-2, Chondromodulin-II, Chm-II, LECT-2, HLECT2, Chm2, LECT2.

    Product # :

    PRO-2037

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    LECT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Gly19-Leu151) containing 143 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 16kDa.

    Source

    Escherichia Coli.

    Formulation

    LECT2 was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl & pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leukocyte Cell-Derived Chemotaxin 2 (LECT2) functions as a chemotactic factor to neutrophils. LECT2 stimulates the proliferation of chondrocytes and osteoblasts. LECT2 is strongly expressed in the liver and weakly in the testis. LECT2 is a secreted, 16kDa protein which serves as a chemotactic factor to neutrophils and stimulates the growth of chondrocytes and osteoblasts. LECT2 protein has a high sequence similarity to the chondromodulin repeat regions of the chicken myb-induced myeloid 1 protein. A polymorphism in the LECT2 gene is linked with rheumatoid arthritis.

    • Synonyms

      Leukocyte Cell-Derived Chemotaxin 2, Leukocyte Cell-Derived Chemotaxin-2, Chondromodulin-II, Chm-II, LECT-2, HLECT2, Chm2, LECT2.

    • 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. LECT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASGPWANICAGK SSNEIRTCDR HGCGQYSAQR SQRPHQGVDI LCSAGSTVYA PFTGMIVGQE KPYQNKNAIN NGVRISGRGF CVKMFYIKPI KYKGPIKKGE KLGTLLPLQK VYPGIQSHVH IENCDSSDPT AYL.

    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.

    Lect2 Human
  • View Data Sheet

    Name :

    LIN28 Human

    Description:

    LIN28 Human Recombinant

    CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    Product # :

    PRO-743

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE

    More Info

    • Introduction

      LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.

    • Synonyms

      CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    • 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 SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.

    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.

    Lin28 Human
  • View Data Sheet

    Name :

    Clusterin Human

    Description:

    Clusterin Human Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    Product # :

    CYT-278

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Clusterin Human Recombinant produced in HEK is a glycosylated, polypeptide chain containing 438 amino acids and having a molecular mass of 51.27 kDa. Clusterin (1-427 a.a.) is fused to 11 a.a. flag tag at c-terminal and purified by proprietary chromatographic techniques.

    Source

    293 cell line (Human embryonic kidney).

    Formulation

    Filtered (0.4 micron) and lyophilized PBS, pH 7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    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 a and b 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 a-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, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Filtered, White, 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 a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Amino Acid Sequence

      DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 51.27kDa.

      What is the source or expression system of CLUSTERIN Protein?
      293 cell line
      What is the Purity of CLUSTERIN Protein?
      CLUSTERIN Protein is >95% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CLUSTERIN Protein?
      DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

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

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

    Clusterin Human Recombinant
  • View Data Sheet

    Name :

    I TAC Human

    Description:

    I-TAC Human Recombinant (CXCL11)

    Small inducible cytokine B11, CXCL11, I-TAC, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.

    Product # :

    CHM-334

    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

    I-TAC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 8300 Dalton. The I-TAC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2?m filtered concentrated (0.5mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.

    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 IL-2 activated T-Lymphocytes using a concentration range of 0.1-10.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokinen family that is also called inducible T-cell alpha chemoattractant (I-TAC) and (IP-9). I-TAC is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. I-TAC is chemotactic for activated T cells. The CXCL11 gene is located on human chromosome 4 along with many other members of the CXC chemokine family.

    • Synonyms

      Small inducible cytokine B11, CXCL11, I-TAC, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      FPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF.

    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.

    I Tac Human
  • View Data Sheet

    Name :

    SPR Human

    Description:

    Sepiapterin Reductase Human Recombinant

    SDR38C1, SPR, Dystonia, Sepiapterin reductase.

    Product # :

    ENZ-411

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Sepiapterin Reductase produced in E.Coli is a single,non-glycosylated polypeptide chain containing 281 amino acids (1-261 a.a.) and having a molecular mass of 30.2 kDa.Sepiapterin Reductase is expressed with a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sepiapterin Reductase is an aldo-keto reductase that catalyzes the NADPH-dependent reduction of pteridine derivatives and is essential in the biosynthesis of BH4. Mutations in Sepiapterin Reductase gene result in DOPA-responsive dystonia due to sepiaterin reductase deficiency defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Sepiapterin reductase is part of the short-chain dehydrogenase/reductase family which reduces exogenous carbonyl compounds as well as phenylpropanedione. Sepiapterin reductase is an important enzyme for the biosynthesis of tetrahydrobiopterin, an necessary cofactor for aromatic amino acid hydrolases together with tyrosine hydroxylase, the rate-limiting enzyme in DOPA synthesis.

    • Synonyms

      SDR38C1, SPR, Dystonia, Sepiapterin reductase.

    • 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 MEGGLGRAVC LLTGASRGFG RTLAPLLASL LSPGSVLVLS ARNDEALRQL EAELGAERSG LRVVRVPADL GAEAGLQQLL GALRELPRPK GLQRLLLINN AGSLGDVSKG FVDLSDSTQV NNYWALNLTS MLCLTSSVLK AFPDSPGLNR TVVNISSLCA LQPFKGWALY CAGKAARDML FQVLALEEPN VRVLNYAPGP LDTDMQQLAR ETSVDPDMRK GLQELKAKGK LVDCKVSAQK LLSLLEKDEF KSGAHVDFYD K.

    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.

    Spr Human
  • View Data Sheet

    Name :

    IL 16 Human, His

    Description:

    Interleukin-16 Human Recombinant, His Tag

    IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

    Product # :

    CYT-562

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (502-631 a.a) containing 150 amino acids and having a molecular mass of 15.5kDa. The IL-16 is fused to a 20 a.a His-Tag at N-Terminus.The IL-16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-16 His tag protein (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM PMSF & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
      IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4.

    • Synonyms

      IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSAGLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS.

    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.

    Il 16 Human His
  • View Data Sheet

    Name :

    IL36RN Human

    Description:

    Interleukin-36 Receptor Antagonist Human Recombinant

    Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

    Product # :

    CYT-009

    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

    IL1F5 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17kDa.The IL1F5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL1F5 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.

    Purity

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

    Biological Activity

    As measured by its binding ability in a functional ELISA, immobilized IL1F5 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.

    More Info

    • Introduction

      Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.

    • Synonyms

      Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL1F5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F5 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 quick spin followed by reconstitution of IL1F5 in PBS to a concentration no less than 100 µg/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 Met-Val-Leu-Ser-Gly.

    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.

    Il1F5 Human
  • View Data Sheet

    Name :

    THYN1 Human

    Description:

    Thymocyte Nuclear Protein 1 Human Recombinant

    MY105, THY28, Thymocyte Protein Thy28, Cyte Nuclear Protein 1.

    Product # :

    PRO-270

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    THYN1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-225a.a.) and having a molecular mass of 27.8kDa.THYN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The THYN1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      THYN1, is greatly conserved among vertebrates and plant types. TYHN1 takes part in the induction of apoptosis. THYN1 in the thymocytes was primarily found in the nucleus, as shown in lymphoma cells, demonstrating that the THYN1 is localized in the nucleus, regardless of the cyclic or resting stage of the cell cycle.

    • Synonyms

      MY105, THY28, Thymocyte Protein Thy28, Cyte Nuclear Protein 1.

    • 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 MSRPRKRLAG TSGSDKGLSG KRTKTENSGE ALAKVEDSNP QKTSATKNCL KNLSSHWLMK SEPESRLEKG VDVKFSIEDL KAQPKQTTCW DGVRNYQARN FLRAMKLGEE AFFYHSNCKE PGIAGLMKIV KEAYPDHTQF EKNNPHYDPS SKEDNPKWSM VDVQFVRMMK RFIPLAELKS YHQAHKATGG PLKNMVLFTR QRLSIQPLTQ EEFDFVLSLE EKEPS

    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.

    Thyn1 Human
  • View Data Sheet

    Name :

    Pleiotrophin Human, His

    Description:

    Pleiotrophin Human Recombinant, His Tag

    PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

    Product # :

    CYT-451

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Pleiotrophin Human Recombinant contains His-Tagged Fusion Protein, produced in E. coli, its molecular weight is 17.3 kDa protein containing 136 amino acid residues of the OSF-1 human and 16 additional amino acid residues - HisTag, thrombin cleavage site (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5 mg/ml in 0.1M phosphate buffer and 0.1M NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pleiotrophin (Osteoblast-Specific Factor-1, OSF-1) contains 136 amino acid residues. The sequence is very rich in cationic amino acids (24% of the residues); lysine cluster sequences are found in the N-terminal and C-terminal ends of the structure.
      The OSF-1 gene was shown by Northern blotting analysis to be expressed in mouse calvarial osteoblast-enriched cells and in mouse brain tissues, but not in thymus, spleen, kidney, liver, lung, testis or heart. Pleiotrophin has the ability to promote adhesion, migration, expansion, and differentiation of human osteoprogenitor cells. In addition to certain types of cancer, the embryonic growth and differentiation factor pleiotrophin is found also in adults in inflammatory diseases. In osteoarthritis, pleiotrophin is especially expressed in early stages, and its concentrations in the synovial fluid could serve as a marker for the progress of the disease. Pleitrophin might be involved in cartilage repair in osteoarthritis, in particular, in earlier stages.

    • Synonyms

      PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add PBS pH 7.2 and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHHM LVPRGSGKKE KPEKKVKKSD CGEWQWSVCV PTSGDCGLGT REGTRTGAEC KQTMKTQRCK IPCNWKKQFG AECKYQFQAW GECDLNTALK TRTGSLKRAL HNAECQKTVT ISKPCGKLTK PKPQAESKKK KKEGKKQEKM LD.

    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.

    Pleiotrophin Human
  • View Data Sheet

    Name :

    Leptin qA Ovine, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Ovine Recombinant

    Product # :

    CYT-1246

    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

    Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant 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 Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

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

    Name :

    Lungkine Mouse

    Description:

    Lungkine (CXCL15) Mouse Recombinant

    C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

    Product # :

    CHM-286

    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 Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

    More Info

    • Introduction

      Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.

    • Synonyms

      C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 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 Lungkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.

    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.

    Lungkine Mouse
  • View Data Sheet

    Name :

    H3N2 Shandong

    Description:

    H3N2 Influenza-A Virus Shandong/9/93

    Product # :

    IHA-004

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • formulation
    • purity
    • More Info

    Description

    Allantoic fluid of 10 days old embryonated eggs, inoculated with influenza A virus, strain A/Shandong/9/93. The Influenza Virus was purified by Ultracentrifugation with 10-40 % sucrose gradient.

    Formulation

    The H3N2A/ Shandong/9/93 solution (1.0mg/ml) contains STE, 0.1% sodium azide (NaN3) and 0.005% thimerosal.

    Stir thoroughly prior to its use.

    Purity

    Greater than 90.0%.

    More Info

    • Introduction

      H3N2 is a subtype of the influenza A virus. Its name derives from the forms of the two kinds of proteinson the surface of its coat, hemagglutinin(H) and neuraminidase(N). H3N2 exchanges genes for internal proteins with other influenza subtypes. H3N2 has tended to dominate in prevalence over H1N1, H1N2, and influenza B. H3N2 strain descended from H2N2by antigenic shift, in which genes from multiple subtypes re-assorted to form a new virus. Both the H2N2and H3N2 strains contained genesfrom avian influenzaviruses.

    • Physical Appearance

      Opaque suspension.

    • Stability

      A/Shandong/9/93 although stable 4°C for 4 weeks, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Inactivation

      Thimerosal and beta propiolactone treatmentThis product has been treated in a manner consistent with methods of inactivation. Generally accepted good laboratory practices appropriate to microbiological/viral safe handling practices and techniques are required at work.

    • Immunological Activity

      Serological studies of influenza A virus, immunogen for antibody production.Tested with anti-influenza A monoclonal antibodies in ELISA.

    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.

    Shangdong 9 93
  • View Data Sheet

    Name :

    Cyclophilin F Rat Bioactive

    Description:

    Cyclophilin-F Rat Recombinant Bioactive

    Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.

    Product # :

    ENZ-1019

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206 a.a) and having a molecular mass of 21.2Da. Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin F protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,300 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmol of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.

    • 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 MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.

    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.

    Cyclophilin F Rat Bioactive
  • View Data Sheet

    Name :

    Eotaxin Mouse

    Description:

    Eotaxin Mouse Recombinant (CCL11)

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

    Product # :

    CHM-308

    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

    Eotaxin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8403.2 Dalton. The CCL11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin in sterile 18MΩ-cm H2O 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 His-Pro-Gly-Ser-Ile.

    • Background

      What is the molecular weight/Mw of EOTAXIN MOUSE Protein?
      EOTAXIN MOUSE Protein has a total Mw of 8.4kDa.

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

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

      What is the Biological Activity of EOTAXIN MOUSE Protein?
      The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.

      What is the amino acid sequence of EOTAXIN MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be His-Pro-Gly-Ser-Ile.

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

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

    Eotaxin Mouse
  • View Data Sheet

    Name :

    IL1RL1 Human, Sf9 Active

    Description:

    Interleukin-1 Receptor Like-1 Human Recombinant, Sf9 Active

    Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 1.

    Product # :

    CYT-1052

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    IL1RL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 318 amino acids (19-328a.a.) and having a molecular mass of 36.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL1RL1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL1RL1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is less or equal to 10ng/ml with IL-33.

    More Info

    • Introduction

      The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.

    • Synonyms

      Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 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

      KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS 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.

    Il1Rl1
  • View Data Sheet

    Name :

    IL2 Canine, His

    Description:

    Interleukin-2 Canine Recombinant, His Tag

    Interleukin-2, IL-2, T-cell growth factor, TCGF.

    Product # :

    CYT-1011

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    IL2 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (21-155 a.a) and having a molecular mass of 18.1 kDa.IL2 Canine is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL2 Canine protein solution (0. 5mg/ml) contains Phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 measured in a cell proliferation assay using CTLL-2 mouse cytotoxic T cells. is < 0.3 ng/ml.

    More Info

    • Introduction

      IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

    • Synonyms

      Interleukin-2, IL-2, T-cell growth factor, TCGF.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAPITS SSTKETEQQM EQLLLDLQLL LNGVNNYENP QLSRMLTFKF YTPKKATEFT HLQCLAEELK NLEEVLGLPQ SKNVHLTDTK ELISNMNVTL LKLKGSETSY NCEYDDETAT ITEFLNKWIT FSQSIFSTLT.

    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.

    Il2 Canine
  • View Data Sheet

    Name :

    IL6 Human, Sf9

    Description:

    Interleukin-6 Human Recombinant, Sf9

    BSF2, HGF, HSF, IFNB2, IL-6.

    Product # :

    CYT-1150

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    IL6 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 189 amino acids (30-212aa) and having a molecular mass of 21.6kDa.(Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL6 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL6 protein (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, determined by cell proliferation assay using TF-1 human erythroleukemic cell, is 0.2 - 0.8 ng/ml . 

    More Info

    • Introduction

      Interleukin-6 or Il-6 is a cytokine with a large assortment of biological functions. IL-6 it has a crucial part in the last differentiation of b-cells into ig-secreting cells. This cytokine also induces myeloma and plasmacytoma growth. Interleukin-6 induces nerve cells differentiation, among hepatocytes it induces acute phase reactants.

    • Synonyms

      BSF2, HGF, HSF, IFNB2, IL-6.

    • 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

      VPPGEDSKDV AAPHRQPLTS SERIDKQIRY ILDGISALRK ETCNKSNMCE SSKEALAENN
      LNLPKMAEKD GCFQSGFNEE TCLVKIITGL LEFEVYLEYL QNRFESSEEQ ARAVQMSTKV
      LIQFLQKKAK NLDAITTPDP TTNASLLTKL QAQNQWLQDM TTHLILRSFK EFLQSSLRAL RQMHHHHHH.

    • Background

      Production and Applications of Human Recombinant Interleukin-6 in Sf9 Cells

      Abstract:

      Interleukin-6 (IL-6) holds a central role in immune regulation, inflammation, and hematopoiesis. The production of Human Recombinant IL-6 using the Sf9 insect cell system presents a versatile approach for investigating its biological functions and potential therapeutic applications. This paper outlines the methodology of producing Human Recombinant IL-6 in Sf9 cells and explores its significance in immunological research and clinical studies.

      Introduction:

      IL-6 is a multifunctional cytokine pivotal in various physiological processes, making it a target of intensive research. The expression of Human Recombinant IL-6 facilitates investigations into its intricate mechanisms and offers potential avenues for therapeutic development. The Sf9 cell system, harnessed from Spodoptera frugiperda, enables efficient recombinant protein expression through baculovirus vectors.

      Methods:

      Production of Human Recombinant IL-6 involves cloning the human IL-6 gene into a baculovirus transfer vector, which is co-transfected with linearized baculovirus DNA into Sf9 cells. The resultant recombinant baculovirus generates and secretes IL-6 into the culture medium. Purification methods, such as chromatography, ensure the protein's quality and functionality.

      Applications:

      Human Recombinant IL-6 from Sf9 cells has broad applications. It serves as a critical tool for investigating IL-6's roles in immune responses, inflammation, and hematopoiesis. Additionally, it plays a crucial role in the development of therapies targeting IL-6-associated disorders like autoimmune diseases, chronic inflammatory conditions, and cancer.

      Sf9 Expression Advantages:

      The Sf9 system offers notable advantages, including post-translational modifications and protein folding, necessary for IL-6's biological activity. Sf9 cells provide a platform for generating properly folded and functional recombinant IL-6, reflecting its native structure and function.

      Challenges and Future Prospects:

      While Sf9-based expression of Human Recombinant IL-6 offers significant advantages, optimization of expression conditions and scale-up strategies remain challenges. Furthermore, the therapeutic potential of Human Recombinant IL-6 requires in-depth preclinical and clinical investigations.

      Conclusion:

      The production of Human Recombinant IL-6 in Sf9 cells through baculovirus expression offers a powerful tool to comprehend IL-6's multifaceted roles in health and disease. This technology is poised to expand our knowledge of IL-6-related conditions and catalyze the development of precision therapeutic interventions.

    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.

    Il6 Human
  • View Data Sheet

    Name :

    IL7R Human

    Description:

    Interleukin-7 Receptor Human Recombinant

    IL7R, Interleukin 7 Receptor, IL-7 Receptor Subunit Alpha, IL-7R Subunit Alpha,CD127 Antigen, IL-7R-Alpha, CDW127, Interleukin-7 Receptor Subunit Alpha, Interleukin 7 Receptor Isoform H5-6, Interleukin 7 Receptor Alpha Chain, IL-7RA,CD127, IL7RA, ILRA.   

    Product # :

    CYT-1046

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    IL7R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (21-239a.a.) and having a molecular mass of 52.5kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). IL7R is expressed with an 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL7R 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

      Interleukin-7 receptor (IL7R) ,is a hematopoietin receptor superfamily member. IL7R takes a vital part in lymphocyte differentiation, proliferation, multiple sclerosis, as well as survival. IL7R protein signaling is vital for T-cell development and regulation of native and memory T-cell homeostasis. Likewise, IL7R is critically needed for the proper function & development of lymphoid cells.

    • Synonyms

      IL7R, Interleukin 7 Receptor, IL-7 Receptor Subunit Alpha, IL-7R Subunit Alpha,CD127 Antigen, IL-7R-Alpha, CDW127, Interleukin-7 Receptor Subunit Alpha, Interleukin 7 Receptor Isoform H5-6, Interleukin 7 Receptor Alpha Chain, IL-7RA,CD127, IL7RA, ILRA.


    • 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

      ADLESGYAQN GDLEDAELDD YSFSCYSQLE VNGSQHSLTC AFEDPDVNIT NLEFEICGAL VEVKCLNFRK LQEIYFIETK KFLLIGKSNI CVKVGEKSLT CKKIDLTTIV KPEAPFDLSV VYREGANDFV VTFNTSHLQK KYVKVLMHDV AYRQEKDENK WTHVNLSSTK LTLLQRKLQP AAMYEIKVRS IPDHYFKGFW SEWSPSYYFR TPEINNSSGE MDLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH 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.

    Il7R Human
  • View Data Sheet

    Name :

    HIV-1 p24, His

    Description:

    HIV-1 p24 Recombinant, His Tag

    Product # :

    HIV-159

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    HIV-1 p24 His Tag Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (155-321 a.a.) and having a molecular mass of 21.2 kDa. The HIV-1 p24 is fused to a 21 amino acid His Tag and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The HIV-1 p24 protein solution contains 20mM Tris-HCl pH-8, 0.1mM PMSF, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The HIV1 p24 His Tag protein performs complex orchestrated tasks during the assembly, budding maturation and infection stages of the viral replication cycle. Throughout viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. HIV-1 P24 gag, the key capsid protein of the HIV-1 virion, is used in clinical trials as one of the components of the HIV-1 vaccine because of the great extent of sequence homology between different isolates.

    • 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 MWVKVVEEKA FSPEVIPMFS ALSEGATPQD LNTMLNTVGG HQAAMQMLKE TINEEAAEWD RLHPVHAGPI APGQMREPRG SDIAGTTSTL QEQIGWMTHN PPIPVGEIYK RWIILGLNKI VRMYSPTSIL DIRQGPKEPF RDYVDRFYKT LRAEQASQEV
      KNWMTETL.

    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.

    Hiv 1 P24 His
  • View Data Sheet

    Name :

    BD 3 Rat

    Description:

    Beta Defensin-3 Rat Recombinant

    Beta-defensin 3, BD-3, Defensin beta 3, Defb3.

    Product # :

    CYT-063

    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

    BD-3 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.5kDa.The BD-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BD-3 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

    More Info

    • Introduction

      Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.

    • Synonyms

      Beta-defensin 3, BD-3, Defensin beta 3, Defb3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.

    • Background

      What is the molecular weight/Mw of BD3 Protein?
      BD3 Protein has a total Mw of 4.5kDa.

      What is the source or expression system of BD3 Protein?
      Escherichia Coli.

      What is the Purity of BD3 Protein?
      BD3 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD3 Protein?
      Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

      What is the amino acid sequence of BD3 Protein?
      KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.

      What applications can BD3 Protein be used in?
      BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD3 Protein?
      The endotoxin level is minimal, BD3 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.

    Bd 3 Rat
  • View Data Sheet

    Name :

    Activin B Human

    Description:

    Activin-B Human Recombinant

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-058

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

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

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

    • Background

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

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

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

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

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

      What applications can ACTIVIN B Protein be used in?

      ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

    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.

    Activin B Human Plant
  • View Data Sheet

    Name :

    Activin B Human Active

    Description:

    Activin-B Human Recombinant, Active

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-057

    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

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

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

    Biological Activity

    The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

    More Info

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.

    • Background

      An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active

      1. Abstract

      Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.

      2. Introduction

      The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.

      3. Structure and Synthesis of Activin-B

      Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.

      4. Biological Functions of Activin-B

      Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.

      5. Activin-B in Regenerative Medicine

      Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.

      6. Activin-B and Reproductive Health

      Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.

      7. Activin-B in Cancer

      Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.

      8. Conclusion and Future Perspectives

      Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

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

      What is the Biological Activity of Activin B Protein?
      The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

    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.

    Activin B Human Active
  • View Data Sheet

    Name :

    CTSW Human

    Description:

    Cathepsin-W Human Recombinant

    Cathepsin W (Lymphopain), LYPN, lymphopain, EC 3.4.22.-.

    Product # :

    ENZ-762

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CTSW Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (22-376) and having a molecular mass of 42.0 kDa. CTSW is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The CTSW solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTSW protein belongs to the peptidase C1 family. CTSW is a cysteine proteinase with a detailed role in the regulation and mechanism of T-cell cytolytic activity. The encoded CTSW is linked to the membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. CTSW expression is up-regulated by interleukin-2.

    • Synonyms

      Cathepsin W (Lymphopain), LYPN, lymphopain, EC 3.4.22.-.

    • 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 MGSIRGPLRA QDLGPQPLEL KEAFKLFQIQ FNRSYLSPEE HAHRLDIFAH NLAQAQRLQE EDLGTAEFGV TPFSDLTEEE FGQLYGYRRA AGGVPSMGRE IRSEEPEESV PFSCDWRKVA GAISPIKDQK NCNCCWAMAA AGNIETLWRI SFWDFVDVSV QELLDCGRCG DGCHGGFVWD AFITVLNNSG LASEKDYPFQ GKVRAHRCHP KKYQKVAWIQ DFIMLQNNEH RIAQYLATYG PITVTINMKP LQLYRKGVIK ATPTTCDPQL VDHSVLLVGF GSVKSEEGIW AETVSSQSQP QPPHPTPYWI LKNSWGAQWG EKGYFRLHRG SNTCGITKFP LTARVQKPDM KPRVSCPP.

    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.

    Ctsw Human
  • View Data Sheet

    Name :

    IL 13 Rat 109 a.a.

    Description:

    Interleukin-13 109 a.a. Rat Recombinant

    NC300, ALRH, BHR1, P600, IL-13.

    Product # :

    CYT-182

    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

    Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids and having a molecular mass of 11.9 kDa. The IL-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized in PBS, pH7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    ED50 range = 40ng/ml, corresponding to a specific activity of > 25,000IU/mg as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.

    More Info

    • Introduction

      IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.

    • Synonyms

      NC300, ALRH, BHR1, P600, IL-13.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 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 Interleukin 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VRRSTSPPVA LRELIEELSN ITQDQKTSLC NSSIVWSVDI TAGGFCAALE SLTNISSCNA IHRTQRILNG LCNQKASDVA SSPPDTKIEV AQFISKLLNY SKQLFRYGH.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 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 IL-13 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.

    Il 13 Rat 109 Aa
  • 1
  • …
  • 36
  • 37
  • 38
  • 39
  • 40
  • …
  • 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.