Search results
1000 results found for “Exendin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
Acrp30 AntibodyDescription:
Adiponectin, Mouse Anti Human
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
ANT-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
- Citations
Formulation
containing PBS, pH-7.4, & 0.1% Sodium Azide
Citations
More Info
-
Introduction
Human Adiponectin is a secreted protein expressed exclusively in differentiated adipocyte (adipokine). Adiponectin contains a modular structure comprising an N-terminal collagenous domain followed by a C-terminal globular domain. APM-1 plays a role in various physiological processes such as energy homeostasis and obesity. Plasma levels of adiponectin are reduced in obese humans, and decreased levels are associated with insulin resistance and hyperinsulinemia.
-
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
-
Physical Appearance
Sterile Filtered solution.
-
Immunogen
Anti-human adiponectin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human adiponectin amino acids 15-244 purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
-
Clone
P1G12AT.
-
Applications
Adiponectin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Recommended dilution range for Western blot analysis is 1:250 ~ 1:1,000. The antibody has the specificity against globular domain of adiponectin. 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
Adiponectin 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.
- View Data Sheet
Name :
Kisspeptin-10Description:
Kisspeptin-10
Product # :
HOR-044Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
- Citations
Description
Kisspeptin-10 Synthetic is a single, non-glycosylated polypeptide chain containing 10 amino acids, having a molecular mass of 1302 Dalton and a Molecular formula of C63H83N17O14 .
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Kisspeptin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kisspeptin-10 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 Kisspeptin-10 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
H-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2.
-
Background
Kisspeptin-10, a peptide derived from the Kisspeptin gene (KISS1), has emerged as a key player in the regulation of reproductive physiology. The peptide is known for its potent ability to stimulate the release of gonadotropin-releasing hormone (GnRH), a crucial factor in the control of the hypothalamic-pituitary-gonadal axis. The pivotal role of kisspeptin-10 in orchestrating the onset of puberty and the regulation of the menstrual cycle highlights its significance in reproductive health. This research aims to delve into the multifaceted functions of kisspeptin-10, shedding light on its physiological roles and potential applications in reproductive disorders.
The primary objective of this study is to comprehensively explore the effects of kisspeptin-10 on the reproductive system. In vitro and in vivo assays will be conducted to investigate the impact of kisspeptin-10 on GnRH release and subsequent gonadotropin secretion. The interactions between kisspeptin-10 and its receptor, G protein-coupled receptor 54 (GPR54), will be explored using binding assays, potentially unraveling novel signaling pathways activated by this interaction.
The second objective is to investigate the potential therapeutic applications of kisspeptin-10 in reproductive disorders. Clinical studies and animal models will be utilized to assess the efficacy of kisspeptin-10 in stimulating ovulation, particularly in cases of infertility caused by hypothalamic dysfunction. Furthermore, the potential of kisspeptin-10 in regulating conditions like polycystic ovary syndrome (PCOS) and hypogonadotropic hypogonadism will be explored.
The third objective is to elucidate the molecular mechanisms underlying the actions of kisspeptin-10. Transcriptomic and proteomic analyses will be employed to identify genes and proteins regulated by kisspeptin-10 stimulation. This information could reveal novel downstream effectors of kisspeptin-10 signaling, contributing to a more comprehensive understanding of its role in reproductive physiology.
By delving into the complexities of kisspeptin-10, this research aims to provide insights into its multifunctional roles in reproductive health and expand its potential therapeutic applications. The findings from this study may pave the way for the development of targeted interventions for reproductive disorders, potentially improving the quality of life for individuals affected by these conditions.
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.
- View Data Sheet
Name :
CTSE HumanDescription:
Cathepsin-E Human Recombinant
Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.
Product # :
ENZ-776Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CTSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (57-363 a.a) and having a molecular mass of 35.4kDa.CTSE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CTSE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinaseexpressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is anoncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variantsencoding different isoforms exist for this gene.
-
Synonyms
Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.
-
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 MGSTESCSMD QSAKEPLINY LDMEYFGTIS IGSPPQNFTV IFDTGSSNLW VPSVYCTSPA CKTHSRFQPS QSSTYSQPGQ SFSIQYGTGS LSGIIGADQV SVEGLTVVGQ QFGESVTEPG QTFVDAEFDG ILGLGYPSLA VGGVTPVFDN MMAQNLVDLP MFSVYMSSNP EGGAGSELIF GGYDHSHFSG SLNWVPVTKQ AYWQIALDNM LWSVPTLTSC RMSPSPLTES PIPSAQLPTP YWTSWMECSS AAVAFKDLTS TLQLGPSGSW GMSSFDSFTQ SLTVGITVWD WPQQSPKEGP CVCACLSDRP
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.
- View Data Sheet
Name :
ANXA5 HumanDescription:
Annexin A5 Human Recombinant
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
Product # :
PRO-732Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
ANXA5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-320 a.a.) and having a molecular mass of 35.9 kDa.ANXA5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA5 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.
-
Synonyms
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
-
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
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI KGDTSGDYKK ALLLLCGEDD.
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.
- View Data Sheet
Name :
CCL24 RatDescription:
Eotaxin-2 Rat Recombinant (CCL24)
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Product # :
CHM-282Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
CCL24 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.2kDa. The CCL24 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.Citations
More Info
-
Introduction
Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3. -
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Rat Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.
-
Background
What is the molecular weight/Mw of CCL24 RAT Protein?
CCL24 RAT Protein has a total Mw of 10.2kDa.
What is the source or expression system of CCL24 RAT Protein?
Escherichia Coli.
What is the Purity of CCL24 RAT Protein?
CCL24 RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL24 RAT Protein?
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL24 RAT Protein?
VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.
What applications can CCL24 RAT Protein be used in?
CCL24 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL24 RAT Protein?
The endotoxin level is minimal, CCL24 RAT Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL24 RAT 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 CCL24 RAT?
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.
- View Data Sheet
Name :
TAC3 HumanDescription:
Tachykinin-3 Human Recombinant
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
Product # :
PRO-716Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy. -
Synonyms
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
-
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 QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.
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.
- View Data Sheet
Name :
Frataxin HumanDescription:
Frataxin Human Recombinant
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
Product # :
PRO-761Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Frataxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (42-210 a.a.) and having a molecular mass of 21.1 kDa. The Frataxin is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Frataxin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Frataxin is a mitochondrial iron binding protein that is part of the FRATAXIN family. Frataxin functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Frataxin plays a role in iron homeostasis. Frataxin is an anti-apoptotic protein which prevents mitochondrial damage and reactive oxygen species (ROS) production.
-
Synonyms
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
-
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 MLRTDIDATC TPRRASSNQR GLNQIWNVKK QSVYLMNLRK SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV SLHELLAAEL TKALKTKLDL SSLAYSGKDA.
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.
- View Data Sheet
Name :
TXN1 HumanDescription:
Thioredoxin Human Recombinant
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Product # :
PRO-569Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 11.7 kDa.
Source
Escherichia Coli.
Formulation
Thioredoxin solution containing 1mg/ml solution containing 1xPBS pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is>150 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.
Citations
More Info
-
Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.
-
Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
-
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
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFFKKGQKVGEFS GANKEKLEAT INELV.
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.
- View Data Sheet
Name :
TXNL1 HumanDescription:
Thioredoxin-Like 1 Human Recombinant
Thioredoxin-like protein 1, TRP32, Txl, 32 kDa thioredoxin-related protein, TXNL, Thioredoxin-like 32kDa, TXL-1.
Product # :
PRO-084Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
TXNL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-289.a.a) and having a molecular mass of 34.4kDa. TXNL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TXNL1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TXNL1 is a cytoplasmic protein which takes part in endocytotic signaling pathways and acts as a redox sensor. TXNL1 is universally expressed in the body and its goal is to couple oxidative stress to endocytosis, thereby regulating the GDI. Moreover, overexpression of TXNL1 inhibits cell proliferation by predisposing the cell to G0/G1 arrest, signifying that TXNL1 also functions as a transcriptional repressor.
-
Synonyms
Thioredoxin-like protein 1, TRP32, Txl, 32 kDa thioredoxin-related protein, TXNL, Thioredoxin-like 32kDa, TXL-1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDTDIP KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDTTFLESD CDEQLLITVA FNQPVKLYSM KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN VNSVTIFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH
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.
- View Data Sheet
Name :
CHGA HumanDescription:
Chromogranin-A Human Recombinant
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-692Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (19-131 a.a) and having a molecular mass of 12.8 kDa. Chromgranin-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein contains 20mM Tris-HCl buffer pH-8, and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
-
Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
-
Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
-
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
MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVME.
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.
- View Data Sheet
Name :
CIAPIN1 HumanDescription:
Cytokine Induced Apoptosis Inhibitor 1 Human Recombinant
DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.
Product # :
PRO-024Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CIAPIN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312 a.a.) and having a molecular mass of 36kDa.CIAPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CIAPIN1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Anamorsin, ( CIAPIN) is a member of anamorsin family. CIAPIN mainly expressed in the cytoplasm of liver, pancreas and heart tissue cells and does not show any homology to known apoptosis regulatory molecules of the Bcl-2 or CASP families, or to signal transduction molecules. CIAPIN1 Expression is reliant on growth factor stimulation. It is a ubiquitously expressed protein, and when it is overexpressed, it grants apoptotic resistance.
-
Synonyms
DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.
-
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 MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA.
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.
- View Data Sheet
Name :
GPN1 HumanDescription:
GPN-loop GTPase 1 Human Recombinant
GPN-loop GTPase 1, XPA binding protein 1 GTPase, RNA polymerase II associated protein 4, MBD2-interacting protein, MBDin, ATP(GTP)-binding protein, XAB1, ATPBD1A, NTPBP, RPAP4.
Product # :
PRO-1140Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
GPN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 398 amino acids (1-374) and having a molecular mass of 44.3 kDa.GPN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPN1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
GPN-loop GTPase 1 (GPN1) is a member of the GPN-loop GTPase family. GPN1 is a guanosine triphosphatase enzyme which has a role in DNA repair and may function in activation of transcription. Small GTPases, which share a biochemical mechanism, act as binary molecular switches and function in the cell is nucleocytoplasmic transport of both proteins and RNA. In addition, GPN1 establishs an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, proposing that it is essential to connect RNA polymerase II to regulators of protein complex formation. GPN1 may also be involved in nuclear localization of XPA.
-
Synonyms
GPN-loop GTPase 1, XPA binding protein 1 GTPase, RNA polymerase II associated protein 4, MBD2-interacting protein, MBDin, ATP(GTP)-binding protein, XAB1, ATPBD1A, NTPBP, RPAP4.
-
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 MGSHMAASAA AAELQASGGP RHPVCLLVLG MAGSGKTTFV QRLTGHLHAQ GTPPYVINLD PAVHEVPFPA NIDIRDTVKY KEVMKQYGLG PNGGIVTSLN LFATRFDQVM KFIEKAQNMS KYVLIDTPGQ IEVFTWSASG TIITEALASS FPTVVIYVMD TSRSTNPVTF MSNMLYACSI LYKTKLPFIV VMNKTDIIDH SFAVEWMQDF EAFQDALNQE TTYVSNLTRS MSLVLDEFYS SLRVVGVSAV LGTGLDELFV QVTSAAEEYE REYRPEYERL KKSLANAESQ QQREQLERLR KDMGSVALDA GTAKDSLSPV LHPSDLILTR GTLDEEDEEA DSDTDDIDHR VTEESHEEPA FQNFMQESMA QYWKRNNK
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.
- View Data Sheet
Name :
CXCL15 MouseDescription:
Lungkine (CXCL15) Mouse Recombinant
C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.
Product # :
CHM-286Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Recombinant Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.Citations
More Info
-
Introduction
Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.
-
Synonyms
C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Lungkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.
-
Background
What is the molecular weight/Mw of CXCL15 MOUSE Protein?
CXCL15 MOUSE Protein has a total Mw of 16.4kDa.
What is the source or expression system of CXCL15 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL15 MOUSE Protein?
CXCL15 MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL15 MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.
What is the amino acid sequence of CXCL15 MOUSE Protein?
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.
What applications can CXCL15 MOUSE Protein be used in?
CXCL15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL15 MOUSE Protein?
The endotoxin level is minimal, CXCL15 MOUSE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL15 MOUSE 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 CXCL15 MOUSE?
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.
- View Data Sheet
Name :
EREG HumanDescription:
Epiregulin Human Recombinant
EREG, Epiregulin, ER.
Product # :
CYT-609Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.Citations
More Info
-
Introduction
Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.
-
Synonyms
EREG, Epiregulin, ER.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epiregulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epiregulin 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 Epiregulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
-
Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 5.6kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.
What is the amino acid sequence of EREG Protein?
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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.
- View Data Sheet
Name :
CFD HumanDescription:
Complement Factor D Human
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
Product # :
PRO-2699Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Human Complement Factor D produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 24kDa.
Source
Human Plasma.
Formulation
CFD protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.
-
Synonyms
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
-
Physical Appearance
Sterile filtered solution.
-
Stability
CFD Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
-
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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.
- View Data Sheet
Name :
Avidin ProteinDescription:
Avidin
Avidin, AVD, AVID.
Product # :
PRO-500Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- biological activity
- More Info
- Citations
Description
Avidin is a glycosylated polypeptide chain having a molecular mass of 68kDa and containing 4 subunits each with a binding site for biotin. The Avidin is purified by affinity chromatographic techniques.The purification procedure ensures minimal contamination by other proteins or DNA.The resulting high activity and purity of the product gives very low non-specific binding (NSB).
Source
Hen's egg white.
Biological Activity
15.0 units/mg protein, 1 unit binds 1µg biotin.
Citations
More Info
-
Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be 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 four to five mannose and three 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 Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution 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 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.
- View Data Sheet
Name :
EGF Long HumanDescription:
Epidermal Growth Factor Long Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-798Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.
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 murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.Citations
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. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.
-
Synonyms
Urogastrone, URG, EGF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long 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 EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
-
Background
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 12.3kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.
What is the amino acid sequence of EGF Protein?
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, 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.
- View Data Sheet
Name :
Adiponectin Human, TrimericDescription:
Adiponectin Human Recombinant, Trimeric form
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-233Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Trimeric form of Adiponectin Human trimeric form was expressed in HEK293 cells. The cysteine 39 was replaced with Alanine (C39A) 9. hAd-C39A can only form a trimer, but not a hexamer or an HMW form.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl, pH 7.4.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.
Citations
More Info
-
Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue.
Many studies demonstrate that Adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle. Attenuate hepatic lipogenesis and gluconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, Adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of Adiponectin activates different signaling pathways and exerts distinct functions. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized Adiponectin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
Add deionized water to a working volume 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
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25 kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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.
- View Data Sheet
Name :
SCGN RatDescription:
Secretagogin Rat Recombinant
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.
Product # :
PRO-657Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa. The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.The Rat SCGN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile filtered concentrated protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas. -
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
-
Solubility
Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
-
Amino Acid Sequence
MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.
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.
- View Data Sheet
Name :
EFNB1 Human, Sf9Description:
Ephrin-B1 Human Recombinant, Sf9
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
Product # :
PRO-2543Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.
-
Synonyms
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PI16 HumanDescription:
Peptidase Inhibitor 16 Human Recombinant
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
Product # :
ENZ-113Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.
-
Synonyms
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized PI16 Human recombinant 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 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
LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.
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.
- View Data Sheet
Name :
TKT HumanDescription:
Transketolase Human Recombinant
Transketolase, TK, TKT1, EC 2.2.1.1.
Product # :
ENZ-588Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
TKT Human Recombinant produced in E. coli is a single polypeptide chain containing 643 amino acids (1-623) and having a molecular mass of 70.0kDa.TKT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TKT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.
-
Synonyms
Transketolase, TK, TKT1, EC 2.2.1.1.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE LLKMFGIDRD AIAQAVRGLI TKA.
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.
- View Data Sheet
Name :
DESI1 HumanDescription:
Desumoylating Isopeptidase 1 Human Recombinant
Desumoylating Isopeptidase 1, Family With Sequence Similarity 152 Member B, PPPDE Peptidase Domain-Containing Protein 2, Desumoylating Isopeptidase 2, FAM152B, PPPDE2, DeSI-1, D15Wsu75e, DESI2, DJ347H13.4, EC 3.4.-.-.
Product # :
ENZ-734Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
DESI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (1-168) and having a molecular mass of 20.7kDa.DESI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DESI1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
DESI1 belongs to the DeSI family and contains 1 PPPDE peptidase domain. This protein is a protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins and has isopeptidase but not SUMO-processing activity. DESI1 desumoylates ZBTB46.
-
Synonyms
Desumoylating Isopeptidase 1, Family With Sequence Similarity 152 Member B, PPPDE Peptidase Domain-Containing Protein 2, Desumoylating Isopeptidase 2, FAM152B, PPPDE2, DeSI-1, D15Wsu75e, DESI2, DJ347H13.4, EC 3.4.-.-.
-
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 MGSMEPPNLY PVKLYVYDLS KGLARRLSPI MLGKQLEGIW HTSIVVHKDE FFFGSGGISS CPPGGTLLGP PDSVVDVGST EVTEEIFLEY LSSLGESLFR GEAYNLFEHN CNTFSNEVAQ FLTGRKIPSY ITDLPSEVLS TPFGQALRPL LDSIQIQPPG GSSVGRPNGQ S
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.
- View Data Sheet
Name :
EEF2K HumanDescription:
Eukaryotic Elongation Factor-2 Kinase Human Recombinant
Eukaryotic Elongation Factor 2 Kinase, Calcium/Calmodulin-Dependent Eukaryotic Elongation Factor 2 Kinase, EEF-2 Kinase, EC 2.7.11.20, EEF-2K, Calcium/Calmodulin-Dependent Eukaryotic Elongation Factor-2 Kinase, Calmodulin-Dependent Protein Kinase III, Eukaroytic Elongation Factor 2 Kinase, Eukaryotic Elongation Factor-2 Kinase, Elongation Factor-2 Kinase, EC 2.7.11, HSU93850, Eukaryotic elongation factor 2 kinase.
Product # :
PKA-061Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
EEF2K Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 748 amino acids (1-725 a.a) and having a molecular mass of 84.6kDa. EEF2K is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EEF2K protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Eukaryotic elongation factor-2 kinase (EEF2K) is threonine kinase which regulates protein synthesis by means of controlling the rate of peptide chain elongation. Upon activation through a diversity of upstream kinases including AMPK or TRPM7, EEF2K phosphorylates the elongation factor EEF2 at a sole site, renders it unable to bind ribosomes and therefore inactive. In turn, the rate of protein synthesis is being reduced.
-
Synonyms
Eukaryotic Elongation Factor 2 Kinase, Calcium/Calmodulin-Dependent Eukaryotic Elongation Factor 2 Kinase, EEF-2 Kinase, EC 2.7.11.20, EEF-2K, Calcium/Calmodulin-Dependent Eukaryotic Elongation Factor-2 Kinase, Calmodulin-Dependent Protein Kinase III, Eukaroytic Elongation Factor 2 Kinase, Eukaryotic Elongation Factor-2 Kinase, Elongation Factor-2 Kinase, EC 2.7.11, HSU93850, Eukaryotic elongation factor 2 kinase.
-
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 MGSMADEDLI FRLEGVDGGQ SPRAGHDGDS DGDSDDEEGY FICPITDDPS SNQNVNSKVN KYYSNLTKSE RYSSSGSPAN SFHFKEAWKH AIQKAKHMPD PWAEFHLEDI ATERATRHRY NAVTGEWLDD EVLIKMASQP FGRGAMRECF RTKKLSNFLH AQQWKGASNY VAKRYIEPVD RDVYFEDVRL QMEAKLWGEE YNRHKPPKQV DIMQMCIIEL KDRPGKPLFH LEHYIEGKYI KYNSNSGFVR DDNIRLTPQA FSHFTFERSG HQLIVVDIQG VGDLYTDPQI HTETGTDFGD GNLGVRGMAL FFYSHACNRI CESMGLAPFD LSPRERDAVN QNTKLLQSAK TILRGTEEKC GSPRVRTLSG SRPPLLRPLS ENSGDENMSD VTFDSLPSSP SSATPHSQKL DHLHWPVFSD LDNMASRDHD HLDNHRESEN SGDSGYPSEK RGELDDPEPR EHGHSYSNRK YESDEDSLGS SGRVCVEKWN LLNSSRLHLP RASAVALEVQ RLNALDLEKK IGKSILGKVH LAMVRYHEGG RFCEKGEEWD QESAVFHLEH AANLGELEAI VGLGLMYSQL PHHILADVSL KETEENKTKG FDYLLKAAEA GDRQSMILVA RAFDSGQNLS PDRCQDWLEA LHWYNTALEM TDCDEGGEYD GMQDEPRYMM LAREAEMLFT GGYGLEKDPQ RSGDLYTQAA EAAMEAMKGR LANQYYQKAE EAWAQMEE.
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.