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  • Cytokines
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  • Tumor Necrosis Factor

    Tumor Necrosis Factor

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  • Adiponectin

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  • AIF1

    AIF1

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    B-Cell Activating Factor

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  • Beta Defensin

    Beta Defensin

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  • Bone Morphogenetic Protein

    Bone Morphogenetic Protein

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  • B type Natriuretic Peptide

    B type Natriuretic Peptide

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  • BST

    BST

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  • Betacellulin

    Betacellulin

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  • Cardiotrophin

    Cardiotrophin

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  • Activin

    Activin

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    VEGF Protein

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  • EGF

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  • Erythropoietin

    Erythropoietin

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  • Insulin-Like Growth Factor

    Insulin-Like Growth Factor

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  • Growth Hormone

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    BCA-1/ BLC (CXCL13)

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    BRAK (CXCL14)

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  • C-10 (CCL6)

    C-10 (CCL6)

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  • Other Chemokines

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  • MEC (CCL28)

    MEC (CCL28)

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  • LD78-beta (CCL3L1)

    LD78-beta (CCL3L1)

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  • CTACK (CCL27)

    CTACK (CCL27)

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  • CXCL16

    CXCL16

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    CXCL17

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    Platelet Factor-4 (CXCL4)

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  • ENA-78 (CXCL5)

    ENA-78 (CXCL5)

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  • Eotaxin (CCL11,24,26)

    Eotaxin (CCL11,24,26)

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    Exodus-2 (CCL21)

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  • Fractalkine (CX3CL1)

    Fractalkine (CX3CL1)

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    Pigment Epithelium-Derived Factor

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  • Actin

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    Complement Component

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    Ag85

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  • Eukaryotic Translation Initiation Factor

    Eukaryotic Translation Initiation Factor

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  • Angiogenin

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  • Ankyrin Repeat Domain

    Ankyrin Repeat Domain

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  • Annexin

    Annexin

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  • Other Natural Proteins

    Other Natural Proteins

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  • Aprotinin

    Aprotinin

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  • Transferrin

    Transferrin

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  • Avidin

    Avidin

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  • Anti Coagulation Factors

    Anti Coagulation Factors

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  • Natural Albumin

    Natural Albumin

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  • Fibronectin

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    Anti Human Heat Shock Protein

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  • Anti Mouse Lymphocyte

    Anti Mouse Lymphocyte

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    Anti Human Chemokine

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  • Anti Viral Monoclonal

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Search results

1000 results found for “Erythropoietin”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    TBCEL Human

    Description:

    Tubulin Folding Cofactor E-Like Human Recombinant

    Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    Product # :

    PRO-030

    Price :

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    Description

    TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TBCEL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

    • Synonyms

      Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    • 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 MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.

    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.

    Tbcel Human
  • View Data Sheet

    Name :

    TECK Human, His

    Description:

    Thymus Expressed Chemokine (CCL25) Human Recombinant, His Tag

    C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.

    Product # :

    CHM-032

    Price :

    Quantity :

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    Description

    TECK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (24-150 a.a.) and having a molecular mass of 16.8kDa.TECK is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
      Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils.

    • Synonyms

      C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.

    • Physical Appearance

      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 MGSHMQGVFE DCCLAYHYPI GWAVLRRAWT YRIQEVSGSC NLPAAIFYLP KRHRKVCGNP KSREVQRAMK LLDARNKVFA KLHHNTQTFQ AGPHAVKKLS SGNSKLSSSK FSNPISSSKR NVSLLISANS GL.

    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.

    Teck Human His
  • View Data Sheet

    Name :

    FLT4 Human

    Description:

    Vascular Endothelial Growth Factor Receptor-3 Human Recombinant

    Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

    Product # :

    PKA-244

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • biological activity
    • More Info

    Description

    Soluble FLT4 Human Recombinant fused with a carboxy-terminal 6X histidine-tag produced in baculovirus is a monomeric, glycosylated, polypeptide containing the extracellular part, 25-774 amino acids and having a total molecular mass of 120 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The FLT4 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT4 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.

    More Info

    • Introduction

      All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

    • Synonyms

      Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 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 FLT4 in sterile water not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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

    Flt4 Human
  • View Data Sheet

    Name :

    TIPIN Human

    Description:

    TIMELESS Interacting Protein Human Recombinant

    TIMELESS Interacting Protein, CSM3 Homolog.

    Product # :

    PRO-1710

    Price :

    Quantity :

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    • description
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    • formulation
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    • More Info

    Description

    TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.

    • Synonyms

      TIMELESS Interacting Protein, CSM3 Homolog.

    • 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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

    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.

    Tipin Human
  • View Data Sheet

    Name :

    Latexin Human

    Description:

    Latexin Human Recombinant

    LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    Product # :

    ENZ-407

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Latexin protein solution contains 20mM Tris-HCl, pH-7.5, 50mM NaCl and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

    • Synonyms

      LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    • 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

      MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYRLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFTFEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDYTILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE.

    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.

    Latexin Human
  • View Data Sheet

    Name :

    TREM2 Human

    Description:

    Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    Product # :

    PRO-1794

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    Description

    TREM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (19-161 a.a) and having a molecular mass of 20.4kDa.TREM2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TREM2 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMHN TTVFQGVAGQ SLQVSCPYDS MKHWGRRKAW CRQLGEKGPC QRVVSTHNLW LLSFLRRWNG STAITDDTLG GTLTITLRNL QPHDAGLYQC QSLHGSEADT LRKVLVEVLA DPLDHRDAGD LWFPGESESF EDAHVEHSIS R.

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

    Trem2 Human
  • View Data Sheet

    Name :

    LXN Mouse

    Description:

    Latexin Mouse Recombinant

    Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.

    Product # :

    PRO-2218

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    Description

    LXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222 a.a) and having a molecular mass of 27.9kDa. LXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LXN protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.

    • Synonyms

      Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.

    • 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 MGSMEIPPTH YAASRAASVA ENCINYQQGT PHKLFLVQTV QQASKEDIPG RGHKYHLKFS VEEIIQKQVT VNCTAEVLYP QMGQGSAPEV NFTFEGEIGK NPDEEDNTFY QSLMSLKRPL EAQDIPDNFG NVSPQMKPVQ HLAWVACGYV MWQNSTEDTW YKMLKIQTVK QVQRNDDFIE LDYTILLHDI ASQEIIPWQM QVLWHPQYGT KVKHNSRLPK EGQAE.

    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.

    Lxn Mouse
  • View Data Sheet

    Name :

    CXCL1 Human

    Description:

    GRO-Alpha Human Recombinant (CXCL1)

    Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    Product # :

    CHM-329

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    Description

    GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM 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 peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.

    • Synonyms

      Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 CXCL1 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 Ala-Ser-Val-Ala-Thr.

    • Background

      What is the molecular weight/Mw of CXCL1 HUMAN Protein?
      CXCL1 HUMAN Protein has a total Mw of 7.81kDa.

      What is the source or expression system of CXCL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL1 HUMAN Protein?
      CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL1 HUMAN Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CXCL1 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.

      What applications can CXCL1 HUMAN Protein be used in?
      CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL1 HUMAN Protein?
      The endotoxin level is minimal, CXCL1 HUMAN 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.

    Gro A Human
  • View Data Sheet

    Name :

    CXCL2 Human

    Description:

    GRO-Beta Human Recombinant (CXCL2)

    Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    Product # :

    CHM-309

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    Description

    GRO-Beta Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7908 Dalton. The CXCL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Biological Activity

    The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

    • Synonyms

      Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Human 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 Ala-Pro-Leu-Ala-Thr.

    • Background

      What is the molecular weight/Mw of CXCL2 HUMAN Protein?
      CXCL2 HUMAN Protein has a total Mw of 7.9kDa.

      What is the source or expression system of CXCL2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL2 HUMAN Protein?
      CXCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL2 HUMAN Protein?
      The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CXCL2 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Leu-Ala-Thr.

      What applications can CXCL2 HUMAN Protein be used in?
      CXCL2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL2 HUMAN Protein?
      The endotoxin level is minimal, CXCL2 HUMAN 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.

    Gro Beta Human
  • View Data Sheet

    Name :

    XRCC3 Human

    Description:

    X-Ray Repair Cross Complementing Protein 3 Human Recombinant

    X-ray repair cross complementing protein 3, RAD51-like.

    Product # :

    PRO-2649

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    Description

    XRCC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (1-346 a.a.) and having a molecular mass of 40 kDa. XRCC3 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The XRCC3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Human X-Ray Repair Cross Complementing Protein 3, also referred to XRCC3, is a member of RecA family and RAD51 subfamily. The protein takes partin homologous recombination to maintain chromosome stability and repair DNA damage. XRCC3functionally complements Chinese hamster irs1SF, a repair-deficient mutant that shows hypersensitivity to a number of different DNA-damaging agents & chromosomally unstable.

    • Synonyms

      X-ray repair cross complementing protein 3, RAD51-like.

    • 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 MDLDLLDLNP RIIAAIKKAK LKSVKEVLHF SGPDLKRLTN LSSPEVWHLL RTASLHLRGS SILTALQLHQ QKERFPTQHQ RLSLGCPVLD ALLRGGLPLD GITELAGRSS AGKTQLALQL CLAVQFPRQH GGLEAGAVYI CTEDAFPHKR LQQLMAQQPR LRTDVPGELL QKLRFGSQIF IEHVADVDTL LECVNKKVPV LLSRGMARLV VIDSVAAPFR
      CEFDSQASAP RARHLQSLGA TLRELSSAFQ SPVLCINQVT EAMEEQGAAH GPLGFWDERV SPALGITWAN QLLVRLLADR LREEEAALGC PARTLRVLSA PHLPPSSCSY TISAEGVRGT PGTQSH

    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.

    Xrcc3 Human
  • View Data Sheet

    Name :

    RNF181 Human

    Description:

    Ring Finger Protein 181 Human Recombinant

    Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    Product # :

    PRO-1218

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    Description

    RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RNF181 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).

    • Synonyms

      Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    • 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 MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.

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    Rnf181 Human
  • View Data Sheet

    Name :

    Procalcitonin Rat

    Description:

    Procalcitonin Rat Recombinant

    Calcitonin, Calca, Calc.

    Product # :

    HOR-019

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    Description

    Procalcitonin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val26-Asn136) containing 121 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 13.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Procalcitonin was filtered (0.4µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 8.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin, Calca, Calc.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASVPLRSTLESS PGMATLSEEE ARLLAALVQN YMQMKVRELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVGA PGKKRDMAKD LETNHHPYFG 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.

    Procalcitonin Rat
  • View Data Sheet

    Name :

    CD105 Human

    Description:

    Endoglin Human Recombinant

    CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    Product # :

    CYT-525

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    Description

    Endoglin Human Recombinant extracellular domain produced in E.Coli is a single, glycosylated, Polypeptide containing 151 amino acids (26-176) and having a molecular mass of 43 kDa.The Endoglin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Endoglin solution in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol.

    Purity

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

    More Info

    • Introduction

      Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
      The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.

    • Synonyms

      CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

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

    • Background

      What is the molecular weight/Mw of CD105 Protein?
      CD105 Protein has a total Mw of 43kDa.

      What is the source or expression system of CD105 Protein?
      Escherichia Coli.

      What is the Purity of CD105 Protein?
      CD105 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD105 Protein?
      The biological functionality of CD105 Protein will be determined in the future.

      What is the amino acid sequence of CD105 Protein?
      CD105 Protein is composed from 151amino acids.

      What applications can CD105 Protein be used in?
      CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD105 Protein?
      The endotoxin level is minimal, CD105 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.

    Endoglin Human
  • View Data Sheet

    Name :

    IL 1 beta Human

    Description:

    Interleukin-1 beta Human Recombinant

    Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    Product # :

    CYT-208

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    Description

    Interleukin-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton.The IL-1 Beta is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-1 Beta was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Phosphate buffer pH=7.1 and 150mM NaCl.

    Purity

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

    Biological Activity

    The specific activity as determined in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.

    More Info

    • Introduction

      Interleukin-1b is produced by activated macrophages, IL-1 Beta stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.

    • Synonyms

      Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 Beta should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin-1b 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 Ala-Pro-Val-Arg-Ser.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.631 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-1 beta Recombinant 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 1 Beta Human
  • View Data Sheet

    Name :

    FGF23 Human

    Description:

    Fibroblast Growth Factor-23 Human Recombinant

    Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    Product # :

    CYT-020

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    Description

    Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

    More Info

    • Introduction

      FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.

    • Synonyms

      Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 FGF-23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

    • Background

      Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.

      Mechanism
      Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.

      Interactions
      Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.

      Function
      Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
      As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.

      Structure
      FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
      Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
      Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.

      What is the molecular weight/Mw of FGF23 HUMAN Protein?
      FGF23 HUMAN Protein has a total Mw of 22.5kDa.

      What is the source or expression system of FGF23 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FGF23 HUMAN Protein?
      FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF23 HUMAN Protein?
      The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

      What is the amino acid sequence of FGF23 HUMAN Protein?
      MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

      What applications can FGF23 HUMAN Protein be used in?
      FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF23 HUMAN Protein?
      The endotoxin level is minimal, FGF23 HUMAN 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.

    Fgf23 Human
  • View Data Sheet

    Name :

    RhD Human

    Description:

    Rh Blood Group D Antigen Human Recombinant

    SLC42A5, CD240D, DIIIc, RhPI, RhII, Rh4.

    Product # :

    PRO-2822

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    Description

    The RhD Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The RhD His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 58 amino acid residues of the RhD Human, 108-165 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      SLC42A5, CD240D, DIIIc, RhPI, RhII, Rh4.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile!

      Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      The Rh blood group system is one of the major blood group systems in humans and the D antigen is the main component of this system.

      D Antigen

      The presence of the D antigen on the surface of red blood cells indicates a positive Rh factor. Individuals with this antigen are classified as Rh-positive (Rh+), while those without it are Rh-negative (Rh-).

      Genetics

      The Rh factor is inherited in a Mendelian manner, with the D antigen being monitored by the RHD gene located on chromosome 1. The presence of the D allele (RHD) results in Rh positivity.

      Immunization

      Rh-negative individuals can develop antibodies against the D antigen if exposed to Rh-positive blood. In order to prevent such interaction, Rh-negative mothers are often given Rh immunoglobulin (Rho(D) immune globulin) during and after pregnancy.

      Clinical Significance

      The Rh D antigen is vital in blood transfusions and pregnancy. Rh incompatibility can occur when an Rh- mother carries an Rh+ fetus, which may lead to hemolytic disease of the newborn (HDN).

      Blood Transfusions

      Rh compatibility is very important in transfusions. Rh- individuals should receive Rh- blood to avoid an immune reaction.

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    Rhd Human
  • View Data Sheet

    Name :

    Buserelin

    Description:

    Buserelin

    Product # :

    HOR-255

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    Description

    Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.

    Formulation

    The Buserelin peptide was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Buserelin
  • View Data Sheet

    Name :

    Ebola Zaire Protein

    Description:

    Ebola Zaire Recombinant Protein

    Product # :

    EVD-078

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    Description

    Nucleoprotein (NP) of Ebola virus has strong antigenicity in immune reactions. C-terminal of EBO-Z nucleoprotein was expressed and purified from E. coli, it migrated at 15kDa on SDS-PAGE and pI is 4.87. Ebola Zaire is fused to a c-terminal his tag and purified by a proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Ebola Zaire protein solution is supplied in Phosphate buffer and 0.02% sodium azide.

    Purity

    >95% pure as determined by 12% SDS-PAGE (Coomassie blue stain).

    More Info

    • Introduction

      Ebolavirus (EVD) belongs to the Filoviridae family of proteins which is comprised of a single-strand, non-infectious RNA genome. EVD genome is about 19,000 base pairs long and covers 7 genes in the order 3'-UTR-NP-VP35-VP40-GP-VP30-VP24-L-5'-UTR. There are 4 different ebolaviruses such as: Zaire (EBO-Z), Sudan (EBO-S), Cote d’Ivoire (EBO-CI) and Reston (EBO-R) that differ in amino acid sequence and location of where the gene overlaps. Similar to filoviruses and ebolavirions, EVD is a filamentous element that could appear in 3 forms: shepherd's crook, U shape or a 6 shape. Ebolaviruses may be coiled, toroid, or branched. Most ebolavirions are 80nm wideand 14,000nm long.

    • 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.

    • Applications

      Immunoassay.

    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.

    Ebola Zaire
  • View Data Sheet

    Name :

    AAMDC Human

    Description:

    Adipogenesis Associated, Mth938 Domain Containing Human Recombinant

    Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.

    Product # :

    PRO-2116

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    Description

    AAMDC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-122 a.a) and having a molecular mass of 15.7 kDa.AAMDC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AAMDC protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adipogenesis Associated, Mth938 Domain Containing, also known as AAMDC is a member of the AAMDC family and takes part in preadipocyte differentiation andadipogenesis.

    • Synonyms

      Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.

    • 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 MGSMTSPEIA SLSWGQMKVK GSNTTYKDCK VWPGGSRTWD WRETGTEHSP GVQPADVKEV VEKGVQTLVI GRGMSEALKV PSSTVEYLKK HGIDVRVLQT EQAVKEYNAL VAQGVRVGGV FHSTC.

    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.

    Aamdc Human
  • View Data Sheet

    Name :

    MIA Human, His

    Description:

    Melanoma Inhibitory Activity Protein Human Recombinant, His Tag

    Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

    Product # :

    CYT-810

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    Description

    MIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (25-131) and having a molecular mass of 14.4 kDa.MIA is fused to a 21 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The MIA solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain. MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.

    • Synonyms

      Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

    • 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 MGPMPKLADR KLCADQECSH PISMAVALQD YMAPDCRFLT IHRGQVVYVF SKLKGRGRLF WGGSVQGDYY GDLAARLGYF PSSIVREDQT LKPGKVDVKT DKWDFYCQ

    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.

    Mia Human His
  • View Data Sheet

    Name :

    HN1 Human

    Description:

    Hematological And Neurological Expressed 1 Human Recombinant

    ARM2, HN1A, Hematological and neurological expressed 1 protein, Androgen-regulated protein 2, HN1.

    Product # :

    PRO-1434

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    Description

    HN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-154) and having a molecular mass of 18.1kDa. HN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HN1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hematological and neurological expressed 1 protein (HN1) is a small protein which is extremely preserved among species. HN1 expression is upregulated in regenerating neural tissues, including the axotomized adult rodent facial motor nerve and dedifferentiating retinal pigment epithelial cells of the Japanese newt. HN1 is also expressed in several tissues during embryonic development as well as in regions of the adult brain which display high plasticity.

    • Synonyms

      ARM2, HN1A, Hematological and neurological expressed 1 protein, Androgen-regulated protein 2, HN1.

    • 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 MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPTEQ PVRKNKMASN IFGTPEENQA SWAKSAGAKS SGGREDLESS GLQRRNSSEA SSGDFLDLKG EGDIHENVDT DLPGSLGQSE EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS LVLG.

    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.

    Hn1 Human
  • View Data Sheet

    Name :

    MYLPF Human

    Description:

    Myosin Light chain, Phosphorylatable, Fast Skeletal Muscle Human Recombinant

    Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    Product # :

    PRO-243

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    Description

    MYLPF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a) and having a molecular mass of 21.2kDa.MYLPF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYLPF protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin regulatory light chains, including MRCL3, MYLPF and MYL9, regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the actin-activated myosin ATPase activity, thus regulating the contractile activity. MYLPF is vital for fast and slow skeletal muscle development.

    • Synonyms

      Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    • 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 MAPKRAKRRT VEGGSSSVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKKFL EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE.

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    Mylpf Human
  • View Data Sheet

    Name :

    Myoglobin His Human

    Description:

    Myoglobin His Human Recombinant

    PVALB, MGC13548.

    Product # :

    PRO-071

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    Description

    MB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154a.a.) and having a molecular mass of 19.3kDa.MB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MB protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myoglobin, mitochondrial precursor is a cytosolic oxygen-binding protein in charge of the storage and diffusion of oxygen within myocytes. The largest expression of MB is in the skeletal and cardiac muscle. MB operates in various functions in muscular oxygen supply, such as oxygen storage, facilitated diffusion, and myoglobin-mediated oxidative phosphorylation.

    • Synonyms

      PVALB, MGC13548.

    • 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 MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKGHPET LEKFDKFKHL KSEDEMKASE DLKKHGATVL TALGGILKKK GHHEAEIKPL AQSHATKHKI PVKYLEFISE CIIQVLQSKH PGDFGADAQG AMNKALELFR KDMASNYKEL GFQG

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    Myoglobin His Human
  • View Data Sheet

    Name :

    APRIL Human

    Description:

    APRIL Human Recombinant

    Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.

    Product # :

    CYT-815

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    • sds-page

    Description

    APRIL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (105-247) and having a molecular mass of 17.6kDa.APRIL is fused to a 16 amino acid T7-tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    APRIL-sds-page - Product image 1

    More Info

    • Introduction

      APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.

    • 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

      MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.

    • Background

      APRIL Human Recombinant: Expanding the Horizons of Immunotherapy

      Abstract:


      APRIL (A Proliferation-Inducing Ligand) is a promising molecule within the tumor necrosis factor (TNF) superfamily that plays a pivotal role in immune regulation. This research paper provides an overview of APRIL human recombinant, exploring its potential applications in immunotherapy. Understanding the mechanisms and therapeutic implications of APRIL holds promise in the field of immune-related disorders. This article presents a concise analysis of APRIL, highlighting its potential as a therapeutic target.

      Introduction:


      Immunotherapy has revolutionized the treatment of various diseases by harnessing the power of the immune system. APRIL, a member of the TNF superfamily, has emerged as a potential candidate for immunotherapeutic interventions. This paper provides an overview of APRIL, shedding light on its structure, function, and potential applications in immunotherapy.

      APRIL Structure and Function:


      APRIL is a transmembrane protein that can be proteolytically cleaved, leading to the generation of soluble forms. It interacts with its receptors, such as BCMA and TACI, to regulate immune responses. APRIL influences B-cell activation, proliferation, and antibody production, making it a compelling target for immunotherapeutic strategies.

      Immunotherapeutic Applications of APRIL Human Recombinant:


      APRIL human recombinant holds great potential in immunotherapy. By modulating APRIL activity, it may be possible to enhance immune responses against cancer cells or dampen immune dysregulation in autoimmune disorders. Additionally, APRIL-based therapeutics could be developed to target specific immune cell populations or enhance the efficacy of existing immunotherapies.

      Challenges and Future Directions:


      Although APRIL shows promise, there are challenges to overcome. Further research is needed to elucidate the precise mechanisms of APRIL-mediated immune regulation and identify optimal therapeutic approaches. Additionally, safety considerations and potential side effects must be thoroughly evaluated.

      Conclusion:


      APRIL human recombinant represents a valuable tool for advancing immunotherapy. Understanding the structure, function, and therapeutic potential of APRIL opens up new avenues for treating immune-related disorders. Continued research and development in this field have the potential to revolutionize the landscape of immunotherapy, improving patient outcomes and expanding the possibilities for personalized medicine.

      What is the molecular weight/Mw of APRIL Protein?
      APRIL Protein has a total Mw of 17.6kDa.

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

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

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

      What is the amino acid sequence of APRIL Protein?
      MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.

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

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

    April Human
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