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Search results

1000 results found for “periostin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    GP9 Human

    Description:

    Glycoprotein-9 Human Recombinant

    Platelet glycoprotein IX, GP-IX, GPIX, Glycoprotein 9, CD42a, Glycoprotein IX (Platelet).

    Product # :

    PRO-055

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    Description

    GP9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (17-147) and having a molecular mass of 16.8kDa. GP9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GP9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycoprotein-9 (GP9) is a small membrane glycoprotein found on the surface of human platelets. GP9 forms a one to one noncovalent complex with glycoprotein Ib, a platelet surface membrane glycoprotein complex which functions as a receptor for von Willebrand factor. The complete receptor complex includes noncovalent association of the alpha and beta subunits with the protein and platelet glycoprotein V. GP9 gene defects cause the Bernard-Soulier syndrome, aka giant platelet disease whose patients have unusually large platelets and have a clinical bleeding tendency.

    • Synonyms

      Platelet glycoprotein IX, GP-IX, GPIX, Glycoprotein 9, CD42a, Glycoprotein IX (Platelet).

    • 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 MGSTKDCPSP CTCRALETMG LWVDCRGHGL TALPALPART RHLLLANNSL QSVPPGAFDH LPQLQTLDVT QNPWHCDCSL TYLRLWLEDR TPEALLQVRC ASPSLAAHGP LGRLTGYQLG SCGWQLQASW VRPG.

    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.

    Gp9 Human
  • View Data Sheet

    Name :

    CIAO1 Human

    Description:

    Cytosolic Iron-Sulfur Protein Assembly 1 Human Recombinant

    CIA1, WDR39, Probable cytosolic iron-sulfur protein assembly protein CIAO1, WD repeat-containing protein 39, CIAO1.

    Product # :

    PRO-1396

    Price :

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    Description

    CIAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-339a.a) and having a molecular mass of 40kDa. CIAO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CIAO1 protein solution (1mg/ml) containing 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

      CIAO1 is a vital component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. CIAO1 protein is required for the maturation of extra mitochondrial Fe/S proteins and seems to specifically modulate the trans-activation activity of WT1. CIAO1 participates in chromosome segregation as a part of the mitotic spindle-associated MMXD complex.

    • Synonyms

      CIA1, WDR39, Probable cytosolic iron-sulfur protein assembly protein CIAO1, WD repeat-containing protein 39, CIAO1.

    • 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 MGSMKDSLVL LGRVPAHPDS RCWFLAWNPA GTLLASCGGD RRIRIWGTEG DSWICKSVLS EGHQRTVRKV AWSPCGNYLA SASFDATTCI WKKNQDDFEC VTTLEGHENE VKSVAWAPSG NLLATCSRDK SVWVWEVDEE DEYECVSVLN SHTQDVKHVV WHPSQELLAS ASYDDTVKLY REEEDDWVCC ATLEGHESTV WSLAFDPSGQ RLASCSDDRT VRIWRQYLPG NEQGVACSGS DPSWKCICTL SGFHSRTIYD IAWCQLTGAL ATACGDDAIR VFQEDPNSDP QQPTFSLTAH LHQAHSQDVN CVAWNPKEPG LLASCSDDGE VAFWKYQRPE 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.

    Ciao1 Human
  • View Data Sheet

    Name :

    CINP Human

    Description:

    Cyclin-Dependent Kinase 2 Interacting Protein Human Recombinant

    Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    Product # :

    PKA-269

    Price :

    Quantity :

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    Description

    CINP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.4 kDa.The CINP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CINP protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.

    • Synonyms

      Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    • Physical Appearance

      CINP is supplied as a 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 MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLLN KDKIELDSSS PASKENEEKV CLEYNEELEK LCEELQATLD GLTKIQVKME KLSSTTKGIC ELENYHYGEE SKRPPLFHTW PTTHFYEVSH KLLEMYRKEL LLKRTVAKEL AHTGDPDLTL SYLSMWLHQP YVESDSRLHL ESMLLETGHR AL

    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.

    Cinp Human
  • View Data Sheet

    Name :

    PSMB9 Human

    Description:

    Proteasome Subunit Beta Type 9 Human Recombinant

    Proteasome subunit beta type-9, Low molecular mass protein 2, Macropain chain 7, Multicatalytic endopeptidase complex chain 7, Proteasome chain 7, Proteasome subunit beta-1i, Really interesting new gene 12 protein, PSMB9, LMP2, PSMB6i, RING12, beta1i, MGC70470.

    Product # :

    ENZ-105

    Price :

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    Description

    PSMB9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (21-219 a.a.) and having a molecular mass of 23.5kDa.PSMB9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PSMB9 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proteasome subunit beta type-9 (PSMB9) belongs to the proteasome B-type family which is a 20S core beta subunit. PSMB9 is positioned in the class II region of the MHC (major histocompatibility complex). Expression of the PSMB9 protein is induced by INFG and this gene product replaces catalytic subunit 1 (proteasome beta 6 subunit) in the immunoproteasome.

    • Synonyms

      Proteasome subunit beta type-9, Low molecular mass protein 2, Macropain chain 7, Multicatalytic endopeptidase complex chain 7, Proteasome chain 7, Proteasome subunit beta-1i, Really interesting new gene 12 protein, PSMB9, LMP2, PSMB6i, RING12, beta1i, MGC70470.

    • 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 MTTIMAVEFD GGVVMGSDSR VSAGEAVVNR VFDKLSPLHE RIYCALSGS AADAQAVADMA AYQLELHGIE LEEPPLVLAA ANVVRNISYK YREDLSAHLM VAGWDQREGG QVYGTLGGML TRQPFAIGGS GSTFIYGYVD AAYKPGMSPE ECRRFTTDAI ALAMSRDGSS GGVIYLVTIT AAGVDHRVIL GNELPKFYDE.

    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.

    Psmb9 Human
  • View Data Sheet

    Name :

    CKS1B Human

    Description:

    CDC28 Protein Kinase Regulatory Subunit 1B Human Recombinant

    CDC28 Protein Kinase Regulatory Subunit 1B, CDC28 Protein Kinase 1B, Cyclin-Dependent Kinases Regulatory Subunit 1, NB4 Apoptosis/Differentiation Related Protein, CDC2-Associated Protein CKS1, Cell Division Control Protein CKS1, CDC28 Protein Kinase 1, PNAS-143, PNAS-16, PNAS-18, CKS-1, ckshs1.

    Product # :

    PRO-1834

    Price :

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    Description

    CKS1B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (1-79) and having a molecular mass of 12.0 kDa. CKS1B is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The CKS1B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CKS1B protein which binds to the catalytic subunit of cyclin dependent kinases is vital for their biological function. The CKS1B mRNA is expressed in HeLa cells during the course of cell cycle in several forms which suggests that the encoded protein has a particular function. Two transcript variants were identified for this gene however it seems that only one of them encodes a protein.

    • Synonyms

      CDC28 Protein Kinase Regulatory Subunit 1B, CDC28 Protein Kinase 1B, Cyclin-Dependent Kinases Regulatory Subunit 1, NB4 Apoptosis/Differentiation Related Protein, CDC2-Associated Protein CKS1, Cell Division Control Protein CKS1, CDC28 Protein Kinase 1, PNAS-143, PNAS-16, PNAS-18, CKS-1, ckshs1.

    • 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 MGSMSHKQIY YSDKYDDEEF EYRHVMLPKD IAKLVPKTHL MSESEWRNLG VQQSQGWVHY MIHEPEPHIL LFRRPLPKKP KK

    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.

    Cks1B Human
  • View Data Sheet

    Name :

    PTGES3 Human

    Description:

    Prostaglandin E Synthase 3 Human Recombinant

    TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.

    Product # :

    ENZ-458

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    Description

    Recombinant Human PTGES3 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 160 amino acids (1-160 a.a.) and having a molecular mass of 18.6 kDa.PTGES3 is purified by convential chromatogrpahy techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTGES3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PTGES3 takes part as a cochaperone and is involved in signal transduction.
      PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.
      PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.

    • Synonyms

      TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.

    • 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

      MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE.

    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.

    Ptges3 Human
  • View Data Sheet

    Name :

    MEIS3 Human

    Description:

    Meis Homeobox 3 Human Recombinant

    Meis Homeobox 3, Meis1-Related Protein 2, MRG2, Meis1, Myeloid Ecotropic Viral Integration Site 1 Homolog 3 (Mouse), Meis1, Myeloid Ecotropic Viral Integration Site 1 Homolog 3, Homeobox Protein Meis3, Homeobox protein Meis3.

    Product # :

    PRO-2121

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    Description

    MEIS3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 41.4kDa. MEIS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MEIS3 protein solution (1 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Meis Homeobox 3, also known as MEIS3 is a member of the TALE/MEIS homeobox family. MEIS3 contains 1 homeobox DNA-binding domain. In addition, MEIS3 is over expressed in the Brain - Amygdala , Uterus , Brain - Anterior cingulate cortex and Brain – Cortex.

    • Synonyms

      Meis Homeobox 3, Meis1-Related Protein 2, MRG2, Meis1, Myeloid Ecotropic Viral Integration Site 1 Homolog 3 (Mouse), Meis1, Myeloid Ecotropic Viral Integration Site 1 Homolog 3, Homeobox Protein Meis3, Homeobox protein Meis3.

    • 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 MGSMARRYDE LPHYPGIVDG PAALASFPET VPAVPGPYGP HRPPQPLPPG LDSDGLKREK DEIYGHPLFP LLALVFEKCE LATCSPRDGA GAGLGTPPGG DVCSSDSFNE DIAAFAKQVR SERPLFSSNP ELDNLMIQAI QVLRFHLLEL EKGKMPIDLVIEDRDGGCRE DFEDYPASCP SLPDQNNMWI RDHEDSGSVH LGTPGPSSGG LASQSGDNSS DQGDGLDTSV ASPSSGGEDE DLDQERRRNK KRGIFPKVAT NIMRAWLFQH LSHPYPSEEQ KKQLAQDTGL TILQVNNWFI NARRRIVQPM IDQSNRTGQG AAFSPEGQPI GGYTETQPHVAVRPPGSVGM SLNLEGEWHY L

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    Meis3 Human
  • View Data Sheet

    Name :

    RLN3 Human

    Description:

    Relaxin-3 Human Recombinant

    Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

    Product # :

    PRO-2176

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    Description

    Relaxin-3 Human Recombinant produced in E.Coli is a disulfide-linked heterodimeric, non-glycosylated, polypeptide chain containing 24 amino acids for A chain and 27 amino acids for B chain and having a molecular mass of 2.5kDa for A chain and 3kDa for B chain.The Relaxin-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by cAMP accumulation in human THP-1 cells, is less than 17.5ng/ml.

    More Info

    • Introduction

      Relaxin-3 (RLN3) belongs to the relaxin family. Relaxins are endocrine and autocrine/paracrine hormones. Relaxin, which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. Unlike human Relaxins 1 and 2, Relaxin 3 does not seem to have a role in reproduction; however it is involved in stress response in the brain stem. RLN3 is the only known ligand for the G-protein-coupled receptor GPCR135, titled RXFP3. In addition, RLN3 binds the LGR7 (RXFP1) receptor, however with lower affinity than Relaxin-2. Even though binding of RLN3 to LGR7 increases intracellular cAMP, binding to GPCR135 suppresses cAMP accumulation, indicating coupling to Gi, Go, or Gz by this receptor.

    • Synonyms

      Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RLN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Relaxin-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized RLN3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      A chain: DVLAGLSSSC CKWGCSKSEI SSLC.
      B chain: RAAPYGVRLCG REFIRAVIFT CGGSRW.

    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.

    Rln3 Human
  • View Data Sheet

    Name :

    Thymosin β4

    Description:

    Thymosin-b4 Human Recombinant

    Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.

    Product # :

    HOR-003

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    Description

    Thymosin b4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 43 amino acids and having a molecular mass of 4.9kDa.The Thymosin b4 Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2um filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    More Info

    • Introduction

      CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.

    • Synonyms

      Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin B4 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymosin B4 Human 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 Thymosin B4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES

    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.

    Thymosin B4
  • View Data Sheet

    Name :

    GM-CSF Poricne, His

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant, His Tag

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

    Product # :

    CYT-1160

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    Description

    GMCSF Poricne Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (18-144a.a.) and having a molecular mass of 16.6kDa.GMCSF is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GMCSF protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

    More Info

    • Introduction

      The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

    • 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 MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

    • Background

      What is the molecular weight/Mw of GM-CSF PORCINE, HIS Protein?
      GM-CSF PORCINE, HIS Protein has a total Mw of 16.6kDa.

      What is the source or expression system of GM-CSF PORCINE, HIS Protein?
      Escherichia Coli.

      What is the Purity of GM-CSF PORCINE, HIS Protein?
      GM-CSF PORCINE, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF PORCINE, HIS Protein?
      The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

      What is the amino acid sequence of GM-CSF PORCINE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

      What applications can GM-CSF PORCINE, HIS Protein be used in?
      GM-CSF PORCINE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GM-CSF PORCINE, HIS Protein?
      The endotoxin level is minimal, GM-CSF PORCINE, HIS Protein was purified using conventional chromatography techniques.


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    Porcine Gm Csf
  • View Data Sheet

    Name :

    EGF Mouse, Biotin

    Description:

    Epidermal Growth Factor Mouse Recombinant, Biotin

    Urogastrone, URG, EGF.

    Product # :

    CYT-841

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

    • Background

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

      Abstract:

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

      Introduction:

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

      Protein Engineering and Biotin Conjugation:

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

      Cellular Signaling Amplification:

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

      Cellular Assays and Functional Responses:

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

      Tailored Delivery Strategies:

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

      Regenerative Medicine and Targeted Therapy:

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

      Future Prospects and Challenges:

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

      Conclusion:

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

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

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

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

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

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

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

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

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

    Egf Mouse Biotin
  • View Data Sheet

    Name :

    CSTB Antibody

    Description:

    Cystatin B, Mouse Anti Human

    Cystatin-B, Stefin-B, Liver thiol proteinase inhibitor, CPI-B, CSTB, CST6, EPM1, PME, STFB.

    Product # :

    ANT-339

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    • More Info

    Formulation

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

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    • Introduction

      Type 1 cystatins are also called stefins which function as intracellular thiol protease inhibitors. Cystatin-B protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. CSTB protein protects proteases leakage from lysosomes. Mutations in Stefin-B gene cause primary defects in patients with progressive myoclonic epilepsy (EPM1), a degenerative disease of the central nervous system. CSTB is overexpressed & elevated in the serum of HCC patients. Cystatin-B in vivo has a polymeric structure which is sensitive to the redox environment. Cystatin-B inhibits bone resorption by down-regulating intracellular cathepsin K activity despite increased osteoclast survival. Protein and mRNA levels of stefin B are significantly lower in atypical benign meningiomas. Stefins-A & Stefin-B which belong to the type-1 Cystatins, are up-regulated in lung tumours and thus able to counteract harmful tumour-associated proteolytic activity. Human stefin-A & Stef

    • Synonyms

      Cystatin-B, Stefin-B, Liver thiol proteinase inhibitor, CPI-B, CSTB, CST6, EPM1, PME, STFB.

    • Immunogen

      Anti-human CSTB mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CSTB amino acids 1-98 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      P2F1AT.

    • Applications

      CSTB 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~ 2,000. Recommended starting dilution 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

      CSTB 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.

    Cstb Antibody
  • View Data Sheet

    Name :

    PRDX6 Antibody

    Description:

    Peroxiredoxin-6, Mouse Anti Human

    Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.

    Product # :

    ANT-581

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    • More Info

    Formulation

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

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    • Introduction

      Peroxiredoxin 6 (PRDX6) belongs to the thiol-specific antioxidant protein family. PRDX6 is a bifunctional enzyme with 2 distinct active sites. PRDX6 is involved in redox regulation of the cell and can reduce Hydrogen peroxide and short chain organic, fatty acid, and phospholipid hydroperoxides. PRDX6 may have a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Furthermore, PRDX6 eases the oxidative stress and TGF-beta-induced abnormalities of human trabecular meshwork cells. In addition, PRDX6 is necessary for blood vessel integrity in injured skin.
      At acidic pH, PRDX6 binds to reduced phospholipids, however at cytosolic pH PRDX6 binds only to phospholipids that are oxidized which is compatible with the role for PRDX6 in the repair of peroxidized cell membranes. Hydrogen peroxide-mediated hyperoxidation of PRDX6 induces cell cycle arrest at the G2/M transition via up-regulation of iPLA2 activity. Overexpression of PRDX6 is linked to oligodendroglioma.

    • Synonyms

      Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PRDX6 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PRDX6 amino acids 1-224 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT22E7AT.

    • Applications

      PRDX6 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      PRDX6 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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    Prdx6 Antibody
  • View Data Sheet

    Name :

    Avidin Recombinant

    Description:

    Avidin Recombinant

    Avidin, AVD, AVID.

    Product # :

    PRO-2597

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    Description

    Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.

    Source

    Corn (Zea Mays).

    Purity

    Greater than 90% as visualized by SDS-PAGE.

    Biological Activity

    13.5 units/mg protein, 1 unit binds 1µg biotin.

    More Info

    • Introduction

      Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

    • Synonyms

      Avidin, AVD, AVID.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Recombinant Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant Avidin 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 Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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.

    Avidin Recombinant
  • View Data Sheet

    Name :

    BD 1 Rat

    Description:

    Beta Defensin -1 Rat Recombinant

    Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.

    Product # :

    CYT-062

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    Description

    BD-1 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4.1kDa.The BD-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BD-1 protein 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.

    Biological Activity

    Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

    More Info

    • Introduction

      The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
      Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
      Beta Defensin is highly expressed by epithelial cells.
      Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.

    • Synonyms

      Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized BD-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

    • Background

      What is the molecular weight/Mw of BD1 Protein?
      BD1 Protein has a total Mw of 4.1kDa.

      What is the source or expression system of BD1 Protein?
      Escherichia Coli.

      What is the Purity of BD1 Protein?
      BD1 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD1 Protein?
      Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

      What is the amino acid sequence of BD1 Protein?
      DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

      What applications can BD1 Protein be used in?
      BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD1 Protein?
      The endotoxin level is minimal, BD1 Protein was purified using conventional chromatography techniques.

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

    Bd 1 Rat
  • View Data Sheet

    Name :

    BD 4 Rat

    Description:

    BD 4 Rat

    Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.

    Product # :

    CYT-066

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    Description

    BD-4 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.4kDa.The BD-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BD-4 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.

    More Info

    • Introduction

      Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
      4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
      Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
      In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

    • Synonyms

      Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized BD-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.

    • Background

      What is the molecular weight/Mw of BD4 Protein?
      BD4 Protein has a total Mw of 4.4kDa.

      What is the source or expression system of BD4 Protein?
      Escherichia Coli.

      What is the Purity of BD4 Protein?
      BD4 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD4 Protein?
      Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.

      What is the amino acid sequence of BD4 Protein?
      QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.

      What applications can BD4 Protein be used in?
      BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD4 Protein?
      The endotoxin level is minimal, BD4 Protein was purified using conventional chromatography techniques.

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

    Bd 4 Rat
  • View Data Sheet

    Name :

    STIP1 Human, His

    Description:

    Stress-Induced-Phosphoprotein 1 Human Recombinant, His Tag

    HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.

    Product # :

    PRO-753

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    Description

    Recombinant Human STIP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543 a.a) and having a molecular mass of 64.8kDa. STIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The STIP1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA, 0.2mM PMSF and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

    • Synonyms

      HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.

    • 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 MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPDWGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLRNKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDKAKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH TPDVLKKCQQAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC QLEPTFIKGYTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.

    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.

    Stip1 Human
  • View Data Sheet

    Name :

    ATF Human

    Description:

    Apo Transferrin Human

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    Product # :

    PRO-325

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    Description

    Human Apo Transferrin is a glycoprotein of approximately 77 kDa.

    Source

    Human serum.

    Formulation

    The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.

    Purity

    Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.

    • Iron Content

      The Iron content was estimated by ICP and was found to be <6 ppm.

    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.

    Apo Transferrin Human
  • View Data Sheet

    Name :

    GM- CSF Human, Sf9

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Sf9

    CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    Product # :

    CYT-416

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    Description

    GM-CSF Human Recombinant produced in insect cells is a single, glycosylated, polypeptide chain containing 127 amino acids (18-144) and having a molecular mass of 14.6kDa. GM-CSF is fused to a C-terminal His -tag (6x His) and purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    The protein was lyophilized with PBS.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor 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-Ala-Arg-Ser.

    • Background

      Recombinant Granulocyte-Macrophage Colony-Stimulating Factor (GMCSF) is a protein that plays a crucial role in the production and differentiation of white blood cells, including granulocytes and macrophages. It is a potent stimulator of hematopoietic stem cells, which are responsible for the production of all blood cells in the body. Recombinant GMCSF is a synthetic version of the protein that is produced using recombinant DNA technology.

      Recombinant GMCSF has been extensively studied for its potential therapeutic applications in a variety of medical conditions, including cancer, autoimmune diseases, and infectious diseases. In cancer, GMCSF is used as an immunostimulatory agent to enhance the immune response against cancer cells. By stimulating the production and differentiation of white blood cells, GM-CSF can increase the number of immune cells that can recognize and attack cancer cells. This approach has been successfully used in the treatment of several types of cancer, including melanoma and leukemia.

      In autoimmune diseases, recombinant GMCSF has been investigated as a potential treatment for conditions such as rheumatoid arthritis and multiple sclerosis. These diseases are characterized by an overactive immune response that attacks healthy tissues in the body. By modulating the immune response, GMCSF may be able to reduce inflammation and prevent further damage to affected tissues.

      In infectious diseases, recombinant GMCSF has been studied as a potential treatment for conditions such as sepsis and HIV/AIDS. In sepsis, a severe bacterial infection, GMCSF may be able to stimulate the production of white blood cells and improve the immune response against the infection. In HIV/AIDS, GMCSF may be able to enhance the immune response against the virus and reduce the risk of opportunistic infections.

      Recombinant GMCSF is typically administered by injection, either directly into the affected tissue or into the bloodstream. It is generally well-tolerated, although some patients may experience side effects such as fever, fatigue, and muscle pain.

      In conclusion, recombinant GMCSF is a promising therapeutic agent with potential applications in a variety of medical conditions. Its ability to stimulate the production and differentiation of white blood cells makes it a valuable tool in the treatment of cancer, autoimmune diseases, and infectious diseases. Ongoing research is likely to uncover new uses for this protein and further refine its therapeutic potential.

      What is the molecular weight/Mw of GM- CSF HUMAN, SF9 Protein?
      GM- CSF HUMAN, SF9 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of GM- CSF HUMAN, SF9 Protein?
      Insect Cells.
      What is the Purity of GM- CSF HUMAN, SF9 Protein?
      GM- CSF HUMAN, SF9 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM- CSF HUMAN, SF9 Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of GM- CSF HUMAN, SF9 Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

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

      What is the endotoxin level for GM- CSF HUMAN, SF9 Protein?
      The endotoxin level is minimal, GM- CSF HUMAN, SF9 Protein was purified using conventional chromatography techniques.


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

    Gm Csf Human Sf9
  • View Data Sheet

    Name :

    Eotaxin Rat

    Description:

    Eotaxin Rat Recombinant (CCL11)

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

    Product # :

    CHM-260

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    • description
    • source
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    Description

    Eotaxin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8.4kDa. The CCL11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in in 1×PBS, pH7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution CCL11 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.

    • Background

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

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

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

      What is the Biological Activity of EOTAXIN RAT Protein?
      Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.

      What is the amino acid sequence of EOTAXIN RAT Protein?
      HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.

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

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


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

    Eotaxin Rat
  • View Data Sheet

    Name :

    CXCL8 Human (1-72)

    Description:

    Interleukin-8 (1-72 a.a.) Human Recombinant (CXCL8)

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    Product # :

    CHM-231

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    Description

    Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 72 amino acids and having a molecular mass of 8452 Dalton. The IL-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL-8 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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-8 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 Ser-Ala-Lys-Glu-Leu.

    • Background

      What is the molecular weight/Mw of CXCL8 HUMAN (1-72) Protein?
      CXCL8 HUMAN (1-72) Protein has a total Mw of 8.45kDa.

      What is the source or expression system of CXCL8 HUMAN (1-72) Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN (1-72) Protein?
      CXCL8 HUMAN (1-72) Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN (1-72) Protein?
      Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CXCL8 HUMAN (1-72) Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.

      What applications can CXCL8 HUMAN (1-72) Protein be used in?
      CXCL8 HUMAN (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN (1-72) Protein?
      The endotoxin level is minimal, CXCL8 HUMAN (1-72) 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.

    Il 8 72 Human
  • View Data Sheet

    Name :

    SCF Rat

    Description:

    Stem Cell Factor Rat Recombinant

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

    Product # :

    CYT-323

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    • description
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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

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

    Scf Rat
  • View Data Sheet

    Name :

    Eotaxin Rhesus Macaque

    Description:

    Eotaxin Rhesus Macaque Recombinant (CCL11)

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    Product # :

    CHM-022

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    Description

    Recombinant Eotaxin Rhesus Macaque produced in E.coli cells is a non-glycosylated, homodimeric protein containing 74 amino acid chain and having a molecular mass of 8.4kDa. The Eotaxin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Eotaxin was lyophilized from a 0.2µm filtered concentrated solution in 2×PBS, pH 7.0.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood eosinophils is in a concentration range of 0.1-10.0 ng/ml corresponding to a specific activity of 1.0 × 105 - 1.0 × 107 IU/mg.

    More Info

    • Introduction

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

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Eotaxin Recombinant in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPDSVATTCC FTLTNKKIPL QRLESYRRII SGKCPQKAVI FKTKLAKDIC ADPKKKWVQD SMKYLDRKSP TPKP

    • Background

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

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

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

      What is the Biological Activity of EOTAXIN RHESUS MACAQUE Protein?
      Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood eosinophils is in a concentration range of 0.1-10.0 ng/ml corresponding to a specific activity of 1.0 × 105 - 1.0 × 107 IU/mg.

      What is the amino acid sequence of EOTAXIN RHESUS MACAQUE Protein?
      GPDSVATTCC FTLTNKKIPL QRLESYRRII SGKCPQKAVI FKTKLAKDIC ADPKKKWVQD SMKYLDRKSP TPKP

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

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


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

    Eotaxin Rhesus Macaque
  • View Data Sheet

    Name :

    IL 9 Mouse

    Description:

    Interleukin-9 Mouse Recombinant

    P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.

    Product # :

    CYT-373

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    Description

    Interleukin-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa. The IL-9 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution 10mM Na2PO4, pH 7.5.

    Purity

    Greater than 96.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of human MO7e cells is < 0.5 ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.

    More Info

    • Introduction

      Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.

    • Synonyms

      P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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 9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQRCSTTWGI RDTNYLIENL KDDPPSKCSC SGNVTSCLCL SVPTDDCTTP CYREGLLQLT NATQKSRLLP VFHRVKRIVE VLKNITCPSF SCEKPCNQTM AGNTMSFLKS LLGTFQKTEM QRQKSRP.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.6 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 IL-9 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.

    Il9 Mouse
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