Search results
1000 results found for “albumin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
Insulin Human (20-110)Description:
Insulin (20-110 a.a) Human Recombinant
Product # :
CYT-1237Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized Insulin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
-
Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
-
Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.
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 :
LIN7B HumanDescription:
LIN7B Human Recombinant
LIN-7B, MALS-2, MALS2, VELI2, Protein lin-7 homolog B, Veli-2, hVeli2, Mammalian lin-seven protein 2, Vertebrate lin-7 homolog 2, UNQ3116/PRO10200.
Product # :
PRO-1298Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
LIN7B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-207 a.a.) and having a molecular mass of 25.3kDa.LIN7B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LIN7B protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE
Citations
More Info
-
Introduction
LIN7B (VELI2), is a member of the Velis family. Velis family contains minor synaptic proteins which interact with other proteins at the post-synaptic density (PSD) of neuronal synapses. Velis which contain the PDZ motif, participate in recruiting cell adhesion molecules, receptors, and channels. Lin7B protein is ubiquitously expressed with a high expression in the brain, liver, and testis. Lin7B localizes at the synaptic junctions in neurons, bind to CASK, which is a neurexin-binding protein highly concentrated in synapses, and Mint1, a binding partner with a vesicle trafficking protein.
-
Synonyms
LIN-7B, MALS-2, MALS2, VELI2, Protein lin-7 homolog B, Veli-2, hVeli2, Mammalian lin-seven protein 2, Vertebrate lin-7 homolog 2, UNQ3116/PRO10200.
-
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 MGSMAALVEP LGLERDVSRA VELLERLQRS GELPPQKLQA LQRVLQSRFC SAIREVYEQL YDTLDITGSA EIRAHATAKA TVAAFTASEG HAHPRVVELP KTDEGLGFNI MGGKEQNSPI YISRVIPGGV ADRHGGLKRG DQLLSVNGVS VEGEQHEKAV ELLKAAQGSV KLVVRYTPRV LEEMEARFEK MRSARRRQQH QSYSSLESRG.
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 :
Activin-A Human Plant-ActiveDescription:
Activin-A Human Recombinant, Plant-Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-414Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana.
Formulation
Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4
Purity
Greater than 98% as obsereved by SDS-PAGE.
Biological Activity
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.Citations
More Info
-
Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
-
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
-
Physical Appearance
Lyophilized freeze dried powder.
-
Stability
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.
-
Solubility
INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.
-
Amino Acid Sequence
HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS. -
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.What is the source or expression system of Activin A Protein?
Nicotiana benthamiana.What is the Purity of Activin A Protein?
Activin A Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LAYN HumanDescription:
Layilin Human Recombinant
Layilin
Product # :
PRO-1629Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
LAYN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (22-235) and having a molecular mass of 26.7kDa.LAYN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LAYN solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
LAYN, also known as Layilin, contains 1 c-type lectin domain. This protein is receptor for hyaluronate and Interacts with NF2, RDX and TLN1. The C-terminal domain interacts with the N-terminal domain of RDX.
-
Synonyms
Layilin
-
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 MGSATGRLLS ASDLDLRGGQ PVCRGGTQRP CYKVIYFHDT SRRLNFEEAK EACRRDGGQL VSIESEDEQK LIEKFIENLL PSDGDFWIGL RRREEKQSNS TACQDLYAWT DGSISQFRNW YVDEPSCGSE VCVVMYHQPS APAGIGGPYM FQWNDDRCNM KNNFICKYSD EKPAVPSREA EGEETELTTP VLPEETQEED AKKTFKESRE AALNLAY
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 :
AMH Human, HEKDescription:
Anti-Mullerian Hormone Human Recombinant, HEK
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
Product # :
PRO-2665Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
AMH Human Recombinant is a single, glycosylated polypeptide chain containing 439 amino acids (19-451a.a) and having a molecular mass of 46.5kDa (calculated). AMH is fused to a 6 a.a His tag at C-terminal.
Source
HEK293
Formulation
AMH filtered (0.4 µm) and lyophilized in PBS and 5% (w/v) trehalose.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Anti-Mullerian Hormone also known as AMH is a member of the TGF-beta family. AMH is a glycoprotein which is produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. AMH inhibits the growth of tumors derived from tissues of Muellerian duct origin. Moreover, AMH participates in Leydig cell differentiation and function in addition to follicular development in adult females.
-
Synonyms
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
-
Amino Acid Sequence
LLGTEALRAE EPAVGTSGLI FREDLDWPPG SPQEPLCLVA LGGDSNGSSS PLRVVGALSA YEQAFLGAVQ RARWGPRDLA TFGVCNTGDR QAALPSLRRL GAWLRDPGGQ RLVVLHLEEV TWEPTPSLRF QEPPPGGAGP PELALLVLYP GPGPEVTVTR AGLPGAQSLC PSRDTRYLVL AVDRPAGAWR GSGLALTLQP RGEDSRLSTA RLQALLFGDD HRCFTRMTPA LLLLPRSEPA PLPAHGQLDT VPFPPPRPSA ELEESPPSAD PFLETLTRLV RALRVPPARA SAPRLALDPD ALAGFPQGLV NLSDPAALER LLDGEEPLLL LLRPTAATTG DPAPLHDPTS APWATALARR VAAELQAAAA ELRSLPGLPP ATAPLLARLL ALCPGGPGGL GDPLRALLLL KALQGLRVEW RGRDPRGPGR AQRHHHHHH
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 :
APOM HumanDescription:
Apolipoprotein-M Human Recombinant
G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.
Product # :
CYT-715Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
- Citations
Description
APOM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (23-188 a.a.) and having a molecular mass of 20.9 kDa. APOM protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
APOM Human solution containing 20mM Tris-HCl pH-8 1mM DTT & 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport. .
-
Synonyms
G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.
-
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 MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.
-
Background
Apolipoprotein-M Human Recombinant: Insights into its Role in Lipid Metabolism and Cardiovascular Health
Abstract:
Apolipoprotein-M (ApoM), a unique member of the apolipoprotein family, has gained significant attention in the field of lipid metabolism and cardiovascular health. This research paper provides a comprehensive analysis of ApoM human recombinant, exploring its structure, function, and potential implications in cardiovascular diseases. Understanding the intricate nature of ApoM sheds light on its significance as a potential biomarker and therapeutic target in cardiovascular disorders. This article presents a concise yet comprehensive examination of ApoM, highlighting its impact on human health.Introduction:
Cardiovascular diseases remain a leading cause of global morbidity and mortality, underscoring the importance of understanding lipid metabolism and its association with cardiovascular health. ApoM, an intriguing apolipoprotein, has emerged as a key player in lipid metabolism and cardiovascular function. This paper delves into the intricate nature of ApoM, elucidating its structure, molecular interactions, and potential roles in cardiovascular diseases.Structure and Function of Apolipoprotein-M:
ApoM exhibits a unique structural configuration, comprising a single membrane-bound alpha-helix and a lipocalin-like domain. It predominantly associates with high-density lipoproteins (HDL) and plays a critical role in HDL metabolism and cholesterol transport. Additionally, ApoM has been implicated in endothelial function, inflammation, and modulation of sphingolipid metabolism.Apolipoprotein-M and Cardiovascular Diseases:
Studies have highlighted the potential involvement of ApoM in cardiovascular diseases, such as atherosclerosis and coronary artery disease. Genetic variations in the ApoM gene and alterations in ApoM levels have been associated with disease development and progression. Understanding the role of ApoM in cardiovascular diseases offers insights into potential therapeutic interventions and diagnostic strategies.Apolipoprotein-M Human Recombinant Production:
The production of ApoM human recombinant is made possible through advanced biotechnological techniques, including recombinant DNA technology and protein expression systems. These methods facilitate large-scale production, purification, and characterization of ApoM, providing opportunities for further research and potential therapeutic applications.Therapeutic Potential of Apolipoprotein-M Human Recombinant:
Exploring the therapeutic potential of ApoM holds promise in the field of cardiovascular disorders. Strategies aimed at modulating ApoM expression or function may contribute to the prevention or treatment of lipid metabolism-related diseases. Furthermore, ApoM may serve as a potential biomarker for risk assessment and monitoring of cardiovascular conditions.Conclusion:
Apolipoprotein-M human recombinant represents a fascinating area of research, shedding light on the role of this protein in lipid metabolism and cardiovascular health. Understanding the structure, function, and genetic implications of ApoM is pivotal in advancing our knowledge and exploring its potential as a therapeutic target. Continued investigation into the mechanisms and signaling pathways involving ApoM will likely pave the way for innovative strategies in the diagnosis, prevention, and treatment of cardiovascular diseases.What is the molecular weight/Mw of APOM Protein?
APOM Protein has a total Mw of 20.9kDa.
What is the source or expression system of APOM Protein?
Escherichia Coli.
What is the Purity of APOM Protein?
APOM Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of APOM Protein?
The biological functionality of APOM Protein will be determined in the future.
What is the amino acid sequence of APOM Protein?
MGSSHHHHHH SSGLVPRGSH MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.
What applications can APOM Protein be used in?
APOM Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOM Protein?
The endotoxin level is minimal, APOM 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 :
AHSG HumanDescription:
Alpha-2-HS-Glycoprotein Human Recombinant
PRO2743, A2HS, AHS, FETUA, HSGA, Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A.
Product # :
PRO-1450Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
AHSG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (19-367 a.a) and having a molecular mass of 39.7kDa (Molecular size on SDS-PAGE will appear higher).AHSG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AHSG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.
-
Synonyms
PRO2743, A2HS, AHS, FETUA, HSGA, Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A.
-
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 MGSAPHGPGL IYRQPNCDDP ETEEAALVAI DYINQNLPWG YKHTLNQIDE VKVWPQQPSG ELFEIEIDTL ETTCHVLDPT PVARCSVRQL KEHAVEGDCD FQLLKLDGKF SVVYAKCDSS PDSAEDVRKV CQDCPLLAPL NDTRVVHAAK AALAAFNAQN NGSNFQLEEI SRAQLVPLPP STYVEFTVSG TDCVAKEATE AAKCNLLAEK QYGFCKATLS EKLGGAEVAV TCTVFQTQPV TSQPQPEGAN EAVPTPVVDP DAPPSPPLGA PGLPPAGSPP DSHVLLAAPP GHQLHRAHYD LRHTFMGVVS LGSPSGEVSH PRKTRTVVQP SVGAAAGPVV PPCPGRIRHF KV.
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 :
APIP HumanDescription:
APAF1 interacting protein Human Recombinant
APAF1 interacting protein, CGI-29, APIP2, Mmrp19, APAF1-interacting protein, MTRu-1-P dehydratase, probable methylthioribulose-1-phosphate dehydratase, CGI29, EC 4.2.1.109, dJ179L10.2, MMRP19.
Product # :
PRO-1186Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
APIP Human Recombinant produced E. coli is a single polypeptide chain containing 266 amino acids (1-242) and having a molecular mass of 29.7kDa.APIP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The APIP solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
APIP catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). APIP has an anti-apoptotic function and inhibits muscle ischemic impairment. APIP inhibits the cytochrome c-dependent and APAF1-mediated cell death.
-
Synonyms
APAF1 interacting protein, CGI-29, APIP2, Mmrp19, APAF1-interacting protein, MTRu-1-P dehydratase, probable methylthioribulose-1-phosphate dehydratase, CGI29, EC 4.2.1.109, dJ179L10.2, MMRP19.
-
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 MGSHMSGCDA REGDCCSRRC GAQDKEHPRY LIPELCKQFY HLGWVTGTGG GISLKHGDEI YIAPSGVQKE RIQPEDMFVC DINEKDISGP SPSKKLKKSQ CTPLFMNAYT MRGAGAVIHT HSKAAVMATL LFPGREFKIT HQEMIKGIKK CTSGGYYRYD DMLVVPIIEN TPEEKDLKDR MAHAMNEYPD SCAVLVRRHG VYVWGETWEK AKTMCECYDY LFDIAVSMKK VGLDPSQLPV GENGIV
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 :
Car b 1.0109Description:
Pollen allergen Car b 1 isoform Recombinant
Pollen allergen Car b 1 isoform, Car b 1, Car b 1.0109.
Product # :
PRO-2284Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Recombinant Pollen allergen Car b 1 isoform produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 18kDa. Car b 1.0109 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Car b 1.0109 is supplied in 20mM HEPES buffer pH-8.0, 20% Glycerol and 200mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Pollen allergen Car b 1 isoform (Car b 1.0109) causes an allergic reaction in humans.
-
Synonyms
Pollen allergen Car b 1 isoform, Car b 1, Car b 1.0109.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
-
Molar extinction coefficient
8940; A280(1mg/ml)=0.477
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 :
BatroxobinDescription:
Batroxobin
Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.
Product # :
PRO-2146Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- More Info
- Citations
Description
Batroxobin, isolated from Bothrops atrox snake venom, has an Mw of approximately 43kDa.
Formulation
The Batroxobin protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Citations
More Info
-
Introduction
Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin. -
Synonyms
Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Store the lyophilized Batroxobin between 2-8°C. Do not freeze!
-
Solubility
It is recommended to reconstitute the lyophilized Batroxobin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.
-
Unit Definition
100BU [Batroxobin Units]=1mg.
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 :
Cyclophilin A MouseDescription:
Cyclophilin A Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
Product # :
ENZ-857Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
Cyclophilin A protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
-
Synonyms
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
-
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 MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.
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 :
CCDC25 HumanDescription:
Coiled-Coil Domain Containing 25 Human Recombinant
Coiled-coil domain-containing protein 25, CCDC25.
Product # :
PRO-1655Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CCDC25 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.9kDa.CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CCDC25 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.
-
Synonyms
Coiled-coil domain-containing protein 25, CCDC25.
-
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 MGSMVFYFTS SSVNSSAYTI YMGKDKYENE DLIKHGWPED IWFHVDKLSS AHVYLRLHKG ENIEDIPKEV LMDCAHLVKA NSIQGCKMNN VNVVYTPWSN LKKTADMDVG QIGFHRQKDV KIVTVEKKVN EILNRLEKTK VERFPDLAAE KECRDREERN EKKAQIQEMK KREKEEMKKK REMDELRSYS SLMKVENMSS NQDGNDSDEF M.
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 :
Thyroglobulin Human, BiotinDescription:
Thyroglobulin Human, Biotinylated
Thyroglobulin, TGN, AITD3, TG.
Product # :
PRO-2563Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).
Source
Native, Isolated from human thyroid glands.
Formulation
Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease. -
Synonyms
Thyroglobulin, TGN, AITD3, TG.
-
Physical Appearance
Sterile Filtered solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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 :
ErbB2 (146-192) HumanDescription:
Tyrosine Kinase ErbB-2 (146-192) Human Recombinant
erbB-2, EC 2.7.10.1, p185erbB2, C-erbB-2.
Product # :
PKA-136Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The ErbB2 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ErbB2 His-Tagged Fusion Protein, produced in E. coli, is a 14kDa protein containing 47 amino acid residues of the ErbB2 Human, 146-192amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Synonyms
erbB-2, EC 2.7.10.1, p185erbB2, C-erbB-2.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized ErbB2 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
-
Background
HER2 / ErbB2 (human epidermal growth factor receptor 2) is a member of the ErbB family of receptor tyrosine kinases. It plays a role in cell signalling related to growth, differentiation and proliferation.
erbB-2 encodes a 185-kDa orphan receptor tyrosine kinase that is constitutively active as a dimer and displays potent oncogenic activity when overexpressed.
ErbB2 works as a receptor that, upon ligand binding activates downstream signalling pathways such as the MAPK and PI3K/AKT pathways, promoting cell proliferation and survival.
The activation of ErbB2 leads to enhanced cell growth and survival, making it critical in normal cellular functions and in the pathogenesis of cancer.
Herstatin, as the product of alternative HER-2 transcript, retains intron 8.
The herstatin mRNA is expressed in normal human fetal kidney and liver, but is at reduced levels relative to p185HER-2 mRNA in carcinoma cells that contain an amplified HER-2 gene. Herstatin appears to be an inhibitor of p185HER-2, because it disrupts dimers, reduces tyrosine phosphorylation of p185, and inhibits the anchorage-independent growth of transformed cells that overexpress HER-2.
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 :
MEP1A HumanDescription:
Meprin A Subunit Alpha Human Recombinant
Meprin A Subunit Alpha, PABA Peptide Hydrolase, N-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Alpha, Meprin A, Alpha (PABA Peptide Hydrolase), Endopeptidase-2, EC 3.4.24.18, PPH Alpha, BA268F1.1 (Meprin A Alpha (PABA Peptide Hydrolase)), EC 3.4.24, PPHA, MEP1A.
Product # :
PRO-2349Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
MEP1A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 589 amino acids (22-601 a.a.) and having a molecular mass of 67.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MEP1A is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MEP1A protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Meprin A subunit alpha (MEP1A) is a single-pass type I membrane protein which is a member of the peptidase M12A family. MEP1A is abundantly expressed in the kidney and intestinal epithelial cells, is secreted into the urinary tract and intestinal lumen, and found in leukocytes and cancer cells under certain conditions. MEP1A is capable of proteolytically degrading extracellular matrix proteins, proteolytically processing bioactive proteins, and has a role in inflammatory processes.
-
Synonyms
Meprin A Subunit Alpha, PABA Peptide Hydrolase, N-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Alpha, Meprin A, Alpha (PABA Peptide Hydrolase), Endopeptidase-2, EC 3.4.24.18, PPH Alpha, BA268F1.1 (Meprin A Alpha (PABA Peptide Hydrolase)), EC 3.4.24, PPHA, MEP1A.
-
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
ADPVPIKYLP EENVHDADFG EQKDISEINL AAGLDLFQGD ILLQKSRNGL RDPNTRWTFP IPYILADNLG LNAKGAILYA FEMFRLKSCV DFKPYEGESS YIIFQQFDGC WSEVGDQHVG QNISIGQGCA YKAIIEHEIL HALGFYHEQS RTDRDDYVNI WWDQILSGYQ HNFDTYDDSL ITDLNTPYDY ESLMHYQPFS FNKNASVPTI TAKIPEFNSI IGQRLDFSAI DLERLNRMYN CTTTHTLLDH CTFEKANICG MIQGTRDDTD WAHQDSAQAG EVDHTLLGQC TGAGYFMQFS TSSGSAEEAA LLESRILYPK RKQQCLQFFY KMTGSPSDRL VVWVRRDDST GNVRKLVKVQ TFQGDDDHNW KIAHVVLKEE QKFRYLFQGT KGDPQNSTGG IYLDDITLTE TPCPTGVWTV RNFSQVLENT SKGDKLQSPR FYNSEGYGFG VTLYPNSRES SGYLRLAFHV CSGENDAILE WPVENRQVII TILDQEPDVR NRMSSSMVFT TSKSHTSPAI NDTVIWDRPS RVGTYHTDCN CFRSIDLGWS GFISHQMLKR RSFLKNDDLI IFVDFEDITH LSQHHHHHH.
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 :
SRGN HumanDescription:
Serglycin Human Recombinant
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
Product # :
PRO-965Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.
-
Synonyms
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
-
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 MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.
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 :
Leptin PufferfishDescription:
Leptin Pufferfish Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-530Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.Citations
More Info
-
Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE
GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE
QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC
-
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 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).
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 :
HirudinDescription:
Hirudin Recombinant
Product # :
PRO-362Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Recombinant Hirudin is derived from yeast and the polypeptide chain contains 65 amino acids and its Mw is 6979.5 Dalton which is identical to natural Hirudin except for the substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63.The Recombinant Hirudin is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Each mg of protein was lyophilized from a sterile solution containing 20mM PBS pH-7 and 2% mannitol.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity was found to be >14,000ATU/mg.Citations
More Info
-
Introduction
Recombinant Hirudin is a potent thrombin inhibitor originally derived from the medicinal leech. Hirudin acts directly on thrombin rather than through other clotting factors. The mechanism of Hirudin-thrombin appears to be unique. The conversion of fibrinogen into fibrin by the serine protease enzyme thrombin is a major event in the final stages of blood coagulation. In the final stages of coagulation prothrombinase converts prothrombin into thrombin. Fibrin is subsequently cross linked by factor XIII to form a blood clot. The primary inhibitor of thrombin in normal blood circulation is antithrombin III. The anticoagulatant activity of hirudin is derived from its ability to inhibit the pro-coagulant activity of thrombin (similar to antithrombin III activity). Hirudin is the strongest natural inhibitor of thrombin. Hirudin binds to and inhibits only the activity of thrombin forms with a specific activity on fibrinogen contrasting to antithrombin III activity. Therefore, hirudin has a thrombolytic activity since it prevents or dissolves the formation of clots and thrombi. Hirudin also has therapeutic significance in blood coagulation disorders, in the treatment of skin hematomas and of superficial varicose veins. Hirudin does not hinder with the biological activity of other serum proteins and can also act on complexed thrombin, thus having an advantage over more common anticoagulants and thrombolytics. It is complicated to extract large quantities of hirudin from natural sources; therefore a method for producing and purifying hirudin using recombinant biotechnology has been developed.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Hirudin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hirudin 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 Hirudin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 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
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
-
Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
-
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 MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
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 :
S100G HumanDescription:
S100 Calcium Binding Protein G Human Recombinant
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
Product # :
PRO-156Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- More Info
- Citations
Description
The Recombinant Human S100G produced in E.coli has a molecular mass of 10.04kDa containing 87 amino acid residues of the human S100G and fused to a 9 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
S100G was filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
Citations
More Info
-
Introduction
S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.
-
Synonyms
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHAS TKKSPEELKRS TKKSPEELKR IFEKYAAKEG DPDQLSKDEL KLLIQAEFPS LLKGPNTLDD LFQELDKNGD GEVSFEEFQV LVKKISQ.
-
Applications
Western blotting.
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 :
MLEC HumanDescription:
Malectin Human Recombinant
Malectin, KIAA0152, Oligosaccharyltransferase Complex Subunit (Non-Catalytic).
Product # :
PRO-1614Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
MLEC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (29-269) and having a molecular mass of 29.1kDa.MLEC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MLEC solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
MLEC is a member of the malectin family and is found on endoplasmic reticulum membrane. MLEC is a carbohydrate-binding protein with a high ligand preference for Glc2-N-glycan. MLEC takes part in the initial stages of protein N-glycosylation.
-
Synonyms
Malectin, KIAA0152, Oligosaccharyltransferase Complex Subunit (Non-Catalytic).
-
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 MGSPGLGVAG VAGAAGAGLP ESVIWAVNAG GEAHVDVHGI HFRKDPLEGR VGRASDYGMK LPILRSNPED QILYQTERYN EETFGYEVPI KEEGDYVLVL KFAEVYFAQS QQKVFDVRLN GHVVVKDLDI FDRVGHSTAH DEIIPMSIRK GKLSVQGEVS TFTGKLYIEF VKGYYDNPKV CALYIMAGTV DDVPKLQPHP GLEKKEEEEE EEEYDEGSNL KKQTNKNRVQ SGPRTPNPYA SDNS
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 :
AFAP1 HumanDescription:
Actin Filament Associated Protein 1 Human Recombinant
Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 1.
Product # :
PRO-1972Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
AFAP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 360 amino acids (250-588) and having a molecular mass of 39.2 kDa.AFAP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AFAP1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Actin Filament Associated Protein 1 (AFAP1) is a Src binding partner. AFAP1 is a possible modulator of actin filament integrity in response to cellular signals, and is also playing a role as an adaptor protein by connecting Src family members to actin filaments. AFAP1 takes partin the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.
-
Synonyms
Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 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 MGCSGPVDSE CPPPPSSPVH KAELEKKLSS ERPSSDGEGV VENGITTCNG KEQVKRKKSS KSEAKGTVSK VTGKKITKII SLGKKKPSTD EQTSSAEEDV PTCGYLNVLS NSRWRERWCR VKDNKLIFHK DRTDLKTHIV SIPLRGCEVI PGLDCKHPLT FRLLRNGQEV AVLEASSSED MGRWIGILLA ETGSSTDPEA LHYDYIDVEM SASVIQTAKQ TFCFMNRRVI SANPYLGGTS NGYAHPSGTA LHYDDVPCIN GSLRGKKPPV ASNGVTGKGK TLSSQPKKAD PAAVVKRTGS NAAQYKYGKN RVEADAKRLQ TKEEELLKRK EALRNRLAQL.
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 :
AFP ProteinDescription:
Alpha Fetoprotein Human Recombinant
Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.
Product # :
PRO-2229Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
AFP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 600 amino acids (19-609a.a.) and having a molecular mass of 67.5kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa). AFP is expressed with a ADP at N-terminus and 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AFP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
-
Synonyms
Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.
-
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
ADPRTLHRNEYGI ASILDSYQCT AEISLADLAT IFFAQFVQEA TYKEVSKMVK DALTAIEKPT GDEQSSGCLE NQLPAFLEEL CHEKEILEKY GHSDCCSQSE EGRHNCFLAH KKPTPASIPL FQVPEPVTSC EAYEEDRETF MNKFIYEIAR RHPFLYAPTI LLWAARYDKI IPSCCKAENA VECFQTKAAT VTKELRESSL LNQHACAVMK NFGTRTFQAI TVTKLSQKFT KVNFTEIQKL VLDVAHVHEH CCRGDVLDCL QDGEKIMSYI CSQQDTLSNK ITECCKLTTL ERGQCIIHAE NDEKPEGLSP NLNRFLGDRD FNQFSSGEKN IFLASFVHEY SRRHPQLAVS VILRVAKGYQ ELLEKCFQTE NPLECQDKGE EELQKYIQES QALAKRSCGL FQKLGEYYLQ NAFLVAYTKK APQLTSSELM AITRKMAATA ATCCQLSEDK LLACGEGAAD IIIGHLCIRH EMTPVNPGVG QCCTSSYANR RPCFSSLVVD ETYVPPAFSD DKFIFHKDLC QAQGVALQTM KQEFLINLVK QKPQITEEQL EAVIADFSGL LEKCCQGQEQ EVCFAEEGQK LISKTRAALG VHHHHHH.
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 :
SERPINA8 HumanDescription:
Serpin Peptidase Inhibitor, Clade A Member 8 Human Recombinant
Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.
Product # :
PRO-1572Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
SERPINA8 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 34-485) containing a total of 462 amino acids, having a molecular mass of 51.0kDa (calculated) and fused to a 2 a.a C-terminal linker and an 8 a.a Flag tag at C-Terminus.The Human SERPINA8 is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Serpin Peptidase Inhibitor, Clade A Member 8 (SERPINA8), which is a pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and cleaved by the enzyme renin in response to lowered blood pressure. The ensuing product, angiotensin I, is at that point cleaved by angiotensin converting enzyme (ACE) to produce the physiologically active enzyme angiotensin II. SERPINA8 protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. SERPINA8 gene mutations are linked with susceptibility to essential hypertension, and may cause renal tubular dysgenesis, which is a severe disorder of renal tubular development. Defects in the SERPINA8 gene are also linked with non-familial structural atrial fibrillation, and inflammatory bowel disease.
-
Synonyms
Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. SERPINA8 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
DRVYIHPFHL VIHNESTCEQ LAKANAGKPK DPTFIPAPIQ AKTSPVDEKA LQDQLVLVAA KLDTEDKLRA AMVGMLANFL GFRIYGMHSE LWGVVHGATV LSPTAVFGTL ASLYLGALDH TADRLQAILG VPWKDKNCTS RLDAHKVLSA LQAVQGLLVA QGRADSQAQL LLSTVVGVFT APGLHLKQPF VQGLALYTPV VLPRSLDFTE LDVAAEKIDR FMQAVTGWKT GCSLTGASVD STLAFNTYVH FQGKMKGFSL LAEPQEFWVD NSTSVSVPML SGMGTFQHWS DIQDNFSVTQ VSFTESACLL LIQPHYASDL DKVEGLTFQQ NSLNWMKKLS PRTIHLTMPQ LVLQGSYDLQ DLLAQAELPA ILHTELNLQK LSNDRIRVGE VLNSIFFELE ADEREPTEST QQLNKPEVLE VTLNRPFLFA VYDQSATALH FLGRVANPLS TART DYKDDD DK.
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.