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1000 results found for “Ephrin”

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  • View Data Sheet

    Description:

    Recombinant Anti Human Epidermal Growth Factor Receptor

    Product # :

    ANT-600

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    Description

    Recombinant Anti Human Epidermal Growth Factor Receptor monoclonal antibody produced in CHO is a glycosylated dimer containing 1326 amino acids and having a molecular mass of 187.2 kDa.

    Source

    CHO.

    Formulation

    The protein 15.6mg/ml solution contains 20mmol/L Na2HPO4- NaH2PO4, 0.005% Tween 80, pH7.0.

    Purity

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

    Biological Activity

    Compared with reference standard, the range of biological activity was found to be 86%.

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile filtered colorless liquid formulation.

    • Stability

      Recombinant EGFR Antibody should be stored between 2-8°C. Please do not freeze.

    • Amino Acid Sequence

      Heavy chain
      QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYNTP
      FTSRLSINKDNSKSQVFFKMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAASTKG
      PSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSS
      VVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPK
      PKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTV
      LHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVK
      GFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEAL
      HNHYTQKSLSLSPGK.
      Light chain
      DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPSRF
      SGSGSGTDFTLSINSVESEDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPPSDEQ
      LKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADY
      EKHKVYACEVTHQGLSSPVTKSFNRGEC.

    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.

    Recombinant Egfr Antibody
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    Description:

    Ipamorelin

    Ipamorelin

    Product # :

    HOR-024

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    Description

    Ipamorelin Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 711.85 Dalton and a Molecular formula of C38H49N9O5.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Introduction

      Ipamorelin is a peptide selective agonist of the ghrelin/growth hormone secretagogue receptor and a growth hormone secretagogue. Ipamorelin is a pentapeptide that was derived from GHRP1. Ipamorelin significantly increases plasma growth hormone levels in both animals and humans. Like pralmorelin and GHRP-6, ipamorelin does not affect prolactin, FSH, LH or TSH levels. However, unlike GHRP2 and GHRP6, but as growth hormone-releasing hormone (GHRH), ipamorelin does not stimulate the secretion of adrenocorticotropic hormone (ACTH) or cortisol, and is highly selective for inducing the secretion only of GH.

    • Synonyms

      Ipamorelin

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Aib-His-D-2-Nal-D-Phe-Lys-NH2.

    • Background

      What is the molecular weight/Mw of IPAMORELIN Protein?
      IPAMORELIN Protein has a total Mw of 0.711kDa.

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

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

      What is the amino acid sequence of IPAMORELIN Protein?
      Aib-His-D-2-Nal-D-Phe-Lys-NH2.

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

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

      Who supplies IPAMORELIN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IPAMORELIN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Ipamorelin
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    Description:

    Nafarelin Acetate

    Product # :

    HOR-248

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    Description

    Nafarelin is a decapeptide containing 9 amino acids Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.Nafarelin is purified by proprietary chromatographic techniques.

    Formulation

    The protein (1mg/ml) 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

      Nafarelin acetate is a synthetic analog of the naturally occurring gonadotropin-releasing hormone (GnRH). Nafarelin stimulates the release of the pituitary gonadotropins, LH and FSH, resulting in a temporary increase of ovarian steroidogenesis.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.

    • Background

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

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

      What is the amino acid sequence of NAFARELIN Protein?
      Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.

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

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

      Who supplies NAFARELIN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of NAFARELIN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Nafarelin
  • View Data Sheet

    Description:

    Endocrine Gland Vascular Endothelial Growth Factor Mouse Recombinant

    PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.

    Product # :

    CYT-825

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    Description

    EG-VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4 and 3% Trehalose.

    Purity

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

    More Info

    • Introduction

      Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.

    • Synonyms

      PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.

    • Background

      What is the molecular weight/Mw of EG-VEGF Protein?
      EG-VEGF Protein has a total Mw of 9.6kDa.

      What is the source or expression system of EG-VEGF Protein?
      Escherichia Coli.

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

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

      What is the amino acid sequence of EG-VEGF Protein?
      AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.

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

      What is the endotoxin level for EG-VEGF Protein?
      The endotoxin level is minimal, EG-VEGF 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.

    Eg Vegf Mouse
  • View Data Sheet

    Description:

    Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant

    eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.

    Product # :

    PRO-253

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    Description

    EIF1AX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-144a.a.) and having a molecular wieght of 18.6kDa. EIF1AX is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF1AX protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 5mM DTT, 200mM NaCl and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF1AX is an important eukaryotic translation initiation factor. EIF1AX is essential for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5'' end of capped RNA. EIF1AP1 is needed for maximal rate of protein biosynthesis. EIF1AX increases ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA (I) to 40 S ribosomal subunits.

    • Synonyms

      eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.

    • 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 MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI

    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.

    Eif1Ax Human
  • View Data Sheet

    Description:

    ELAV Like Neuron-Specific RNA Binding Protein 2 Human Recombinant

    ELAV Like Neuron-Specific RNA Binding Protein 2, HUB, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2 (Hu Antigen B), Nervous System-Specific RNA-Binding Protein Hel-N1, Hu-Antigen B, HELN1, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2, ELAV-Like Neuronal Protein 1 Isoform Hel-N2, ELAV-Like Neuronal Protein 1, ELAV-Like Protein 2, Hu Antigen B, HEL-N1, ELAV-like protein 2, ELAV-like neuronal protein 1, Hu-antigen B.

    Product # :

    PRO-2155

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    Description

    ELAVL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 369 amino acids (1-346 a.a) and having a molecular mass of 40.4kDa. ELAVL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ELAVL2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ELAV Like Neuron-Specific RNA Binding Protein 2, also known as ELAVL2 is a neural-specific RNA-binding protein which is recognized with his ability to bind to several 3' UTRs, as well as its own and in addition those of FOS and ID. ELAVL2 identify a GAAA motif in the RNA. One of the diseases associated with ELAVL2 is contagious pustular dermatitis.

    • Synonyms

      ELAV Like Neuron-Specific RNA Binding Protein 2, HUB, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2 (Hu Antigen B), Nervous System-Specific RNA-Binding Protein Hel-N1, Hu-Antigen B, HELN1, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2, ELAV-Like Neuronal Protein 1 Isoform Hel-N2, ELAV-Like Neuronal Protein 1, ELAV-Like Protein 2, Hu Antigen B, HEL-N1, ELAV-like protein 2, ELAV-like neuronal protein 1, Hu-antigen B.

    • 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 MGSMETQLSN GPTCNNTANG PTTINNNCSS PVDSGNTEDS KTNLIVNYLP QNMTQEELKS LFGSIGEIES CKLVRDKITG QSLGYGFVNY IDPKDAEKAI NTLNGLRLQT KTIKVSYARP SSASIRDANL YVSGLPKTMT QKELEQLFSQ YGRIITSRIL VDQVTGISRG VGFIRFDKRI EAEEAIKGLN GQKPPGATEP ITVKFANNPS QKTNQAILSQ LYQSPNRRYP GPLAQQAQRF RFSPMTIDGM TSLAGINIPG HPGTGWCIFV YNLAPDADES ILWQMFGPFG AVTNVKVIRD FNTNKCKGFG FVTMTNYDEA AMAIASLNGY RLGDRVLQVS FKTNKTHKA.

    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.

    Elavl2 Human
  • View Data Sheet

    Description:

    Elongator Acetyltransferase Complex Subunit 4 Human Recombinant

    Elongator complex protein 4, ELP4, Elongator Acetyltransferase Complex Subunit 4, hELP4, PAX6 neighbor gene protein, C11orf19, PAXNEB, dJ68P15A.1, PAX6NEB.

    Product # :

    PRO-2102

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    Description

    ELP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424 a.a.) and having a molecular mass of 49kDa.ELP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ELP4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Elongator Acetyltransferase Complex Subunit 4, also known as ELP4 is a protein coding gene which is a subunit of the RNA polymerase II elongator complex. ELP4 complements phenotypes of yeast ELP4 deletion mutants and is related to Rolandic epilepsy.

    • Synonyms

      Elongator complex protein 4, ELP4, Elongator Acetyltransferase Complex Subunit 4, hELP4, PAX6 neighbor gene protein, C11orf19, PAXNEB, dJ68P15A.1, PAX6NEB.

    • 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 MGSMAAVATC GSVAASTGSA VATASKSNVT SFQRRGPRAS VTNDSGPRLV SIAGTRPSVR NGQLLVSTGL PALDQLLGGG LAVGTVLLIE EDKYNIYSPL LFKYFLAEGI VNGHTLLVAS AKEDPANILQ ELPAPLLDDK CKKEFDEDVY NHKTPESNIK MKIAWRYQLL PKMEIGPVSS SRFGHYYDAS KRMPQELIEA SNWHGFFLPE KISSTLKVEP CSLTPGYTKL LQFIQNIIYE EGFDGSNPQK KQRNILRIGI QNLGSPLWGD DICCAENGGN SHSLTKFLYV LRGLLRTSLS ACIITMPTHL IQNKAIIARV TTLSDVVVGL ESFIGSERET NPLYKDYHGL IHIRQIPRLN NLICDESDVK DLAFKLKRKL FTIERLHLPP DLSDTVSRSS KMDLAESAKR LGPGCGMMAG GKKHLDF.

    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.

    Elp4 Human
  • View Data Sheet

    Description:

    BAFF (BLyS) Receptor Human Recombinant, HEK

    TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

    Product # :

    CYT-1224

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    Description

    BAFFR Human Recombinant is a single, glycosylated, polypeptide chain (1-78 a.a) containing a total of 314 amino acids and having a molecular mass of 34.4 kDa. BAFFR is fused to 233 a.a hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The BAFFR solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

    More Info

    • Synonyms

      TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

    • 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

      DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

    • Background

      B-cell Activating Factor (BAFF) and its corresponding receptor, BAFF-R, are integral components of the immune system, orchestrating crucial processes in B-cell survival, maturation, and differentiation. As we delve into the intricate world of immunology, the study of BAFF and its receptor has unveiled essential pathways that govern the immune responses in health and disease. This research investigates the multifaceted role of BAFF Receptor Protein, shedding light on its structural complexities, signaling mechanisms, and its pivotal contributions to immune regulation. By exploring the interactions between BAFF and its receptor, scientists aim to decipher the delicate balance that underlies immune homeostasis and explore potential therapeutic avenues.

      Structural Architecture of BAFF Receptor Protein:

      BAFF Receptor, a transmembrane protein predominantly expressed on B cells, belongs to the tumor necrosis factor receptor (TNFR) superfamily. Its intricate structure involves various domains, each playing a unique role in ligand binding, receptor activation, and downstream signaling. Understanding the structural intricacies of BAFF Receptor is paramount to unraveling the molecular events that govern B-cell fate decisions and immune responses.

      Physiological Significance in B-Cell Biology:

      BAFF Receptor, upon binding with its ligand BAFF, initiates a cascade of events critical for B-cell survival and function. This interaction promotes B-cell maturation, prevents premature apoptosis, and influences the formation of immune synapses. Additionally, BAFF Receptor signaling is tightly regulated to prevent excessive B-cell activation, ensuring immune tolerance and preventing autoimmune responses. Disruptions in these pathways can lead to autoimmune disorders, underscoring the crucial role of BAFF Receptor in maintaining immune equilibrium.

      Regulation of Immune Responses:

      BAFF Receptor signaling not only affects B-cell development but also has broader implications for immune responses. By modulating antibody production, B-cell activation, and immune memory, BAFF Receptor plays a vital role in shaping adaptive immunity. Its dysregulation has been implicated in various autoimmune conditions, making it an attractive target for therapeutic interventions aimed at restoring immune balance.

      BAFF Receptor as a Therapeutic Target:

      The intricate involvement of BAFF Receptor in autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, has positioned it as a promising therapeutic target. Researchers are exploring monoclonal antibodies and other targeted therapies that aim to modulate BAFF Receptor signaling, providing a new frontier in autoimmune disease management. Additionally, understanding the BAFF-BAFF Receptor axis offers potential insights into the development of vaccines and immunotherapies, fostering innovative approaches in the fight against infectious diseases and malignancies.

      BAFF Receptor Protein, as a key player in immune regulation, embodies the complexities of immunology. Its interactions with BAFF orchestrate fundamental processes in B-cell biology and adaptive immunity. As scientists unravel the intricate signaling pathways and structural nuances of BAFF Receptor, they pave the way for novel therapeutic strategies and innovative treatments for autoimmune disorders and beyond. This research not only deepens our understanding of immune regulation but also holds the promise of transformative advancements in immunotherapy, ultimately shaping the future of immune-related healthcare.

      What is the molecular weight/Mw of BAFF-R Protein?
      BAFF-R Protein has a total Mw of 34.4kDa.

      What is the source or expression system of BAFF-R Protein?
      HEK293 Cells.

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

      What is the Biological Activity of BAFF-R Protein?
      The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

      What is the amino acid sequence of BAFF-R Protein?
      DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

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

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

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

    Baff Receptor Human
  • View Data Sheet

    Description:

    Pigment Epithelium-Derived Factor Human Recombinant, HEK

    Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    Product # :

    CYT-553

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    Description

    PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.The Human PEDF is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    The filtered (0.4µm) concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
      Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
      Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
      PEDF & VEGF genes contribute to the development of diabetic retinopathy.
      PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
      PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
      SerpinF1 is a new promising approach for the treatment of osteosarcoma.
      Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
      VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
      Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
      PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.

    • Synonyms

      Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    • 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.

    • Solubility

      It is recomnded to add deionized water to a working concentration of 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 in the cell culture.

    • Amino Acid Sequence

      QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPAAADYKDDDDK.

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    Serpinf1 Human Hek
  • View Data Sheet

    Description:

    Endothelial-Monocyte Activating Polypeptide II Human Recombinant

    AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

    Product # :

    CYT-607

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    Description

    EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.

    Purity

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

    Biological Activity

    Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

    More Info

    • Introduction

      EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.

    • Synonyms

      AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

    • Background

      What is the molecular weight/Mw of EMAP II HUMAN Protein?
      EMAP II HUMAN Protein has a total Mw of 18.3kDa.

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

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

      What is the Biological Activity of EMAP II HUMAN Protein?
      Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

      What is the amino acid sequence of EMAP II HUMAN Protein?
      SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

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

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

    Emap Ii
  • View Data Sheet

    Description:

    Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant

    PK1, PRK1, Prokineticin 1, EG-VEGF.

    Product # :

    CYT-338

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    Description

    EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.

    More Info

    • Introduction

      Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.

    • Synonyms

      PK1, PRK1, Prokineticin 1, EG-VEGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.

    • Background

      Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications

      Abstract:


      Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent.

      Introduction:


      Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders.

      Production and Characterization:


      Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF.

      Role in Endocrine Disorders:


      EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases.

      Therapeutic Implications:


      Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies.

      Conclusion:


      Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.

      What is the molecular weight/Mw of EG-VEGF Protein?
      EG-VEGF Protein has a total Mw of 9.7kDa.

      What is the source or expression system of EG-VEGF Protein?
      Escherichia Coli.

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

      What is the Biological Activity of EG-VEGF Protein?
      The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.

      What is the amino acid sequence of EG-VEGF Protein?
      AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.

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

      What is the endotoxin level for EG-VEGF Protein?
      The endotoxin level is minimal, EG-VEGF 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.

    Eg Vegf Human
  • View Data Sheet

    Description:

    Fibronectin Type III And Ankyrin Repeat Domains 1 Human Recombinant

    Fibronectin Type 3 And Ankyrin Repeat Domains 1, 1700007B22Rik.

    Product # :

    PRO-1768

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    Description

    FANK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a) and having a molecular mass of 40.7kDa.FANK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FANK1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FANK1 was localized in the nuclei of identical cells in the seminiferous epithelium. Depending on its nuclear localization, a gene ontology analysis proposes that FANK1 has a DNA binding activity therefor operates as a transcription factor. The extremely controlled expression of FANK1, suggests that it takes part in regulating gene expression in the transition from the meiotic phase to the haploid phase throughout spermatogenesis.

    • Synonyms

      Fibronectin Type 3 And Ankyrin Repeat Domains 1, 1700007B22Rik.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEPQKIM PPSKPHPPVV GKVTHHSIEL YWDLEKKAKR QGPQEQWFRF SIEEEDPKMH TYGIIYTGYA TKHVVEGLEP RTLYRFRLKV TSPSGECEYS PLVSVSTTRE PISSEHLHRA VSVNDEDLLV RILQGGRVKV DVPNKFGFTA LMVAAQKGYT RLVKILVSNG TDVNLKNGSG KDSLMLACYA GHLDVVKYLR RHGASWQARD LGGCTALHWA ADGGHCSVIE WMIKDGCEVD VVDTGSGWTP LMRVSAVSGN QRVASLLIDA GANVNVKDRN GKTPLMVAVL NNHEELVQLL LDKGADASVK NEFGKGVLEM ARVFDRQSVV SLLEERKKKQ RPKKSCVC

    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.

    Fank1 Human
  • View Data Sheet

    Description:

    TMEFF1 Human Recombinant

    C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.

    Product # :

    PRO-1429

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    Description

    TMEFF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 314 amino acids (40-330) and having a molecular mass of 33.9kDa. TMEFF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TMEFF1 solution (0.25mg/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

      TMEFF1 is a type I transmembrane glycoprotein which includes 2 follistatin modules and an EGF domain in its extracellular domain, a transmembrane domain and a short cytoplasmic tail. The extracellular domain of TMEFF1 can be released as a soluble protein. TMEFF1 is primarily expressed in brain, but is downregulated in brain neoplasms. TMEFF1 selectively regulates nodal but not activin signaling through direct binding to the nodal co-receptor, Cripto. TMEFF inhibits NODAL and BMP signaling through neural patterning and also a possible tumor suppressor in brain cancers.

    • Synonyms

      C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.

    • 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 MGSSNQPPGG GGGSGGDCPG GKGKSINCSE LNVRESDVRV CDESSCKYGG VCKEDGDGLK CACQFQCHTN YIPVCGSNGD TYQNECFLRR AACKHQKEIT VIARGPCYSD NGSGSGEGEE EGSGAEVHRK HSKCGPCKYK AECDEDAENV GCVCNIDCSG YSFNPVCASD GSSYNNPCFV REASCIKQEQ IDIRHLGHCT DTDDTSLLGK KDDGLQYRPD VKDASDQRED VYIGNHMPCP ENLNGYCIHG KCEFIYSTQK ASCRCESGYT GQHCEKTDFS ILYVVPSRQK LTHV.

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    Tmeff1 Human
  • View Data Sheet

    Description:

    Epidermal Growth Factor, His Active Mouse Recombinant

    AI790464, Pro-epidermal growth factor, URG.

    Product # :

    CYT-1054

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    • SDS-PAGE

    Description

    EGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (977-1029 a.a) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EGF protein solution (0.25mg/ml) contains 10% glycerol, 20mM Tris-HCl (pH 8.0), 0.1M NaCl & 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using mouse Balb/3T3 cell. The ED50 for this effect less or equal to 1ng/ml.

    SDS-PAGE

    More Info

    • Introduction

      Pro-Epidermal Growth Factor Isoform 1 or EGF, is a globular peptide (77aa residues) which includes three intra molecular disulfide bonds. This protein acts as a growth factor that mediates the growth and proliferation of different epithelial & epidermal cells. Among other processes that EGF is part of are inhibition of gastric secretion and wound healing. EGF is a ligand for class I tyrosine kinase receptor (c-erbB).

    • Synonyms

      AI790464, Pro-epidermal growth factor, URG.

    • 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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

    • Background

      Deciphering Epidermal Growth Factor Signaling: Unveiling the Potential of His-Tagged Active Mouse Recombinant

      Abstract:

      This research paper delves into the intricate realm of Epidermal Growth Factor (EGF) signaling, focusing on the novel application of Histidine (His)-tagged Active Mouse Recombinant EGF. By employing sophisticated methodologies encompassing protein engineering, receptor binding assays, and cellular response analyses, this study sheds light on the multifaceted molecular attributes and therapeutic prospects of this innovative variant.

      Introduction:

      Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper delves into the intricate signaling dynamics of EGF, with a spotlight on the innovative approach of utilizing His-Tagged Active Mouse Recombinant EGF to unravel its complexities and therapeutic potential.

      Protein Engineering and His-Tag Integration:

      The study embarks on strategic protein engineering, introducing a Histidine (His) Tag to the Active Mouse Recombinant EGF. This His-Tag facilitates purification and subsequent analyses, enabling a comprehensive exploration of EGF signaling.

      Receptor Binding Assays and Ligand Interaction:

      Advanced receptor binding assays unravel the nuances of EGF's interaction with its cognate receptor, including affinities and kinetics. By employing His-Tagged EGF, the study dissects the impact of the tag on receptor binding, shedding light on its potential implications on downstream signaling.

      Cellular Responses and Pathway Activation:

      In vitro cellular assays unveil the complex web of signaling pathways triggered by EGF. The study employs high-throughput techniques to investigate the intricate cascades initiated by His-Tagged Active Mouse Recombinant EGF, providing insights into its potential role in cell proliferation, migration, and survival.

      Structural Dynamics and Conformational Insights:

      In-depth biophysical analyses, including nuclear magnetic resonance (NMR) spectroscopy, delve into the structural dynamics of His-Tagged EGF. This sheds light on potential conformational changes induced by the tag and their impact on receptor binding affinity.

      Therapeutic Implications and Future Prospects:

      The integration of a His Tag not only facilitates purification but also offers avenues for targeted therapies. His-Tagged EGF could serve as a platform for tailored drug delivery, enhancing the precision of interventions in various pathologies.

      Challenges and Future Research Directions:

      While the His Tag offers immense potential, challenges such as potential interference with receptor binding warrant scrutiny. Future research should focus on optimizing the positioning of the tag and exploring its impact on downstream signaling cascades.

      Conclusion:

      In a synthesis of innovative methodologies and visionary insights, the integration of a His Tag into Active Mouse Recombinant EGF emerges as a paradigm-shifting approach. This technique not only enriches our understanding of EGF signaling dynamics but also presents exciting prospects for personalized therapeutic interventions.

      What is the molecular weight/Mw of EGF MOUSE, HIS ACTIVE Protein?
      EGF MOUSE, HIS ACTIVE Protein has a total Mw of 8.6kDa.

      What is the source or expression system of EGF MOUSE, HIS ACTIVE Protein?
      Escherichia Coli.

      What is the Purity of EGF MOUSE, HIS ACTIVE Protein?
      EGF MOUSE, HIS ACTIVE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of EGF MOUSE, HIS ACTIVE Protein?
      Measured in a cell proliferation assay using mouse Balb/3T3 cell. The ED50 for this effect less or equal to 1ng/ml.

      What is the amino acid sequence of EGF MOUSE, HIS ACTIVE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
      What applications can EGF MOUSE, HIS ACTIVE Protein be used in?
      EGF MOUSE, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EGF MOUSE, HIS ACTIVE Protein?
      The endotoxin level is minimal, EGF MOUSE, HIS ACTIVE 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.

    Epidermal Growth Factor
  • View Data Sheet

    Description:

    Proheparin-Binding EGF-like Growth Factor Rat Recombinant

    Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.

    Product # :

    CYT-170

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    • More Info

    Description

    HB-EGF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa.The HB-EGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filtered (0.2µm) and lyophilized from a concentrated solution containing PBS, 300mM NaCl, pH 7.4 and 5% trehalose.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.

    More Info

    • Introduction

      HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind heparin and heparin sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

    • Synonyms

      Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.

    • Background

      What is the molecular weight/Mw of HB-EGF Protein?
      HB-EGF Protein has a total Mw of 9.7kDa.

      What is the source or expression system of HB-EGF Protein?
      Escherichia Coli.

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

      What is the Biological Activity of HB-EGF Protein?
      The ED50 as determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.

      What is the amino acid sequence of HB-EGF Protein?
      DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.

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

      What is the endotoxin level for HB-EGF Protein?
      The endotoxin level is minimal, HB-EGF 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.

    Hb Egf Rat
  • View Data Sheet

    Name :

    EGFP

    Description:

    Enhanced Green Fluorescent Protein Recombinant

    Green fluorescent protein, GFP.

    Product # :

    PRO-1606

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    Description

    Recombinant EGFP produced in E.coli cells is a single non-glycosylated protein containing 239 amino acid chain and having a molecular mass of 26.9kDa. EGFP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EGFP was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4.

    Purity

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

    More Info

    • Introduction

      GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.

    • Synonyms

      Green fluorescent protein, GFP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EGFP although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution EGFP should be stored at 40C between 2-7 days and for future use below -180C.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 EGFP in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK

    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.

    Egfp
  • View Data Sheet

    Description:

    Endoglin Human Recombinant, His-Tag

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

    Product # :

    CYT-823

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    • sds-page

    Description

    Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    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 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG

    • Background

      What is the molecular weight/Mw of CD105 Protein?
      CD105 Protein has a total Mw of 64.9kDa.

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

      What is the Purity of CD105 Protein?
      CD105 Protein is >85% 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?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG

      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 His
  • View Data Sheet

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    • Activity

    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    More Info

    • Introduction

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

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

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

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

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

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

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

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

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

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

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 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 standard solution of Brain-derived Neurotrophic Factor 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.

    Bdnf Human
  • View Data Sheet

    Description:

    E-selectin Human Recombinant

    E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    Product # :

    PRO-380

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    Description

    E-Selectin Human Recombinant is expressed in E. coli containing amino acids 179-557 fused to an amino terminal hexahistidine tag, having a total molecular weight of 45.22 kDa.

    Source

    Escherichia Coli.

    Formulation

    E-Selectin is supplied in 1x PBS and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.

    • Synonyms

      E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    • Physical Appearance

      Sterile Filtered liquid formulation.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

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

    E Selectin Human
  • View Data Sheet

    Description:

    Eukaryotic Translation Initiation Factor 2 Subunit 1 Alpha, Mouse Anti Human

    Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.

    Product # :

    ANT-059

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    More Info

    • Introduction

      EIF2S1 participates in the premature steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA which binds to a 40S ribosomal subunit, followed by mRNA binding to create a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 should exchange with GTP by way of a reaction catalyzed by eIF-2B.

    • Synonyms

      Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.

    • Immunogen

      Anti-human EIF2S1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EIF2S1 amino acids 1-315 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and kappa light chain.

    • Clone

      PEIF2S1AT.

    • Applications

      EIF2S1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
      Recommended dilution range for Western blot analysis is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      EIF2S1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Eif2S1 Antibody
  • View Data Sheet

    Description:

    Apolipoprotein-J Mouse Recombinant

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

    Product # :

    CYT-1172

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    Description

    Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.

    Source

    HEK293

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Clusterin also known as 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 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, 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.
      Clusterin is up/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 (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 50.2kDa.

      What is the source or expression system of CLUSTERIN Protein?
      HEK293

      What is the Purity of CLUSTERIN Protein?
      CLUSTERIN Protein is >90% 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?
      EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

      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 Mouse
  • View Data Sheet

    Name :

    Glycinin

    Description:

    Allergen Ara h 3.0101 Recombinant

    Glycinin, Arah3.

    Product # :

    ALR-008

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    Description

    Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.

    • Synonyms

      Glycinin, Arah3.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Glycinin
  • View Data Sheet

    Description:

    Hexarelin

    Product # :

    HOR-288

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    Description

    Hexarelin has 7 amino acids H-His-D-2-Methyl-Trp-Ala-Trp-D-Phe-Lys-NH2 and having a molecular weight of 887 Dalton. The Molecular Formula is C47H58N12O6.

    Formulation

    The Hexarelin 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

      Hexarelin stimulates GH secretion. Hexarelin is more resistant to proteolytic degradation than GHRP-6.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      What is the molecular weight/Mw of HEXARELIN Protein?
      HEXARELIN Protein has a total Mw of 0.887kDa.

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

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

      What is the amino acid sequence of HEXARELIN Protein?
      HEXARELIN Protein is composed from 7 amino acids.

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

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

      Who supplies HEXARELIN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of HEXARELIN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Hexarelin
  • View Data Sheet

    Description:

    Epithelial Cell Adhesion Molecule, Mouse Anti Human

    Epithelial cell adhesion molecule, Ep-CAM, Adenocarcinoma-associated antigen, Cell surface glycoprotein Trop-1, Epithelial cell surface antigen, Epithelial glycoprotein, EGP, Epithelial glycoprotein 314, EGP314, hEGP314, KS 1/4 antigen, KSA, Major gastrointestinal tumor-associated protein GA733-2, Tumor-associated calcium signal transducer 1, CD326, EPCAM, GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1, ESA, MK-1, DIAR5, EGP-2, EGP40, KS1/4, HNPCC8.

    Product # :

    ANT-525

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    • formulation
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    Formulation

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

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    • Introduction

      EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.

    • Synonyms

      Epithelial cell adhesion molecule, Ep-CAM, Adenocarcinoma-associated antigen, Cell surface glycoprotein Trop-1, Epithelial cell surface antigen, Epithelial glycoprotein, EGP, Epithelial glycoprotein 314, EGP314, hEGP314, KS 1/4 antigen, KSA, Major gastrointestinal tumor-associated protein GA733-2, Tumor-associated calcium signal transducer 1, CD326, EPCAM, GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1, ESA, MK-1, DIAR5, EGP-2, EGP40, KS1/4, HNPCC8.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human EPCAM mAb, clone PAT37F9AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human EPCAM protein 24-265 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT36F10AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:500.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      EPCAM antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Epcam Antibody