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Description:

Interleukin-6 Signal Transducer Human Recombinant

Interleukin 6 signal transducer, oncostatin M receptor, IL6ST, CD130, CDw130, GP130, GP130-RAPS, IL6R-beta

Product # :

CYT-1156

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Description

IL6ST Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 605 amino acids (23-619 a.a) and having a molecular mass of 68.9kDa.IL6ST is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL6ST solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Interleukin-6 Signal Transducer or IL6ST is a receptor, part of the family of class 1 cytokine receptor. IL6ST binds to IL-6 through membrane-anchored or soluble IL-6R starts a connection between another complex of IL6ST and IL-6 , thus forming a homo-dimer and a signal transduction occurs.
Synonyms
Interleukin 6 signal transducer, oncostatin M receptor, IL6ST, CD130, CDw130, GP130, GP130-RAPS, IL6R-beta
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
ELLDPCGYIS PESPVVQLHS NFTAVCVLKE KCMDYFHVNA NYIVWKTNHF TIPKEQYTII NRTASSVTFT DIASLNIQLT CNILTFGQLE QNVYGITIIS GLPPEKPKNL SCIVNEGKKM RCEWDRGRET HLETNFTLKS EWATHKFADC KAKRDTPTSC TVDYSTVYFV NIEVWVEAEN ALGKVTSDHI NFDPVYKVKP NPPHNLSVIN SEELSSILKL TWTNPSIKSV IILKYNIQYR TKDASTWSQI PPEDTASTRS SFTVQDLKPF TEYVFRIRCM KEDGKGYWSD WSEEASGITY EDRPSKAPSF WYKIDPSHTQ GYRTVQLVWK TLPPFEANGK ILDYEVTLTR WKSHLQNYTV NATKLTVNLT NDRYVATLTV RNLVGKSDAA VLTIPACDFQ ATHPVMDLKA FPKDNMLWVE WTTPRESVKK YILEWCVLSD KAPCITDWQQ EDGTVHRTYL RGNLAESKCY LITVTPVYAD GPGSPESIKA YLKQAPPSKG PTVRTKKVGK NEAVLEWDQL PVDVQNGFIR NYTIFYRTII GNETAVNVDS SHTEYTLSSL TSDTLYMVRM AAYTDEGGKD GPEFTFTTPK FAQGEIELEH HHHHH
Background
Significance of Human Recombinant Interleukin-6 Signal Transducer: Insights and Implications
Abstract:
The Interleukin-6 (IL-6) signal transducer holds a pivotal role in the complex IL-6 signaling pathway, orchestrating crucial cellular responses. This paper delves into the significance of Human Recombinant IL-6 Signal Transducer in unraveling IL-6-mediated cellular communication and highlights its potential applications in research and therapeutic development. The review sheds light on the methodology of producing this transducer and its relevance in advancing our understanding of cytokine signaling.
Introduction:
IL-6, a pleiotropic cytokine, is known to exert its diverse effects through a complex signaling cascade, wherein the signal transducer plays a crucial role. The availability of Human Recombinant IL-6 Signal Transducer enables the investigation of its role in health and disease. This transducer is vital for transmitting IL-6 signals, influencing processes like immune response, inflammation, and cell differentiation.
IL-6 Signal Transduction Pathway:
The IL-6 signal transduction pathway involves binding of IL-6 to its receptor, leading to the recruitment of the signal transducer and subsequent activation of downstream signaling molecules such as JAK/STAT pathway. This orchestrated response modulates gene expression, thereby impacting cellular behavior.
Methods of Production:
Human Recombinant IL-6 Signal Transducer is produced by expressing the corresponding gene in a suitable expression system, often utilizing bacterial or mammalian cells. Proper post-translational modifications are necessary to ensure its biological activity and appropriate functioning within the signaling cascade.
Applications in Research:
Human Recombinant IL-6 Signal Transducer serves as a fundamental tool in elucidating IL-6-mediated signaling mechanisms. Its availability facilitates the exploration of how aberrant signaling contributes to diseases such as autoimmune disorders, inflammatory conditions, and certain cancers. The transducer's interaction with other signaling pathways is also of interest for comprehensive pathway analysis.
Therapeutic Implications:
Understanding the IL-6 signal transduction pathway has led to the development of targeted therapies for IL-6-related diseases. Modulation of this pathway presents potential opportunities for novel therapeutic interventions, thereby offering a new dimension in precision medicine.
Challenges and Future Directions:
While the availability of Human Recombinant IL-6 Signal Transducer has significantly advanced our knowledge, challenges remain in deciphering the intricate nuances of IL-6 signaling. Developing strategies to selectively intervene in this pathway without disturbing physiological homeostasis presents an ongoing challenge.
Conclusion:
The Human Recombinant IL-6 Signal Transducer serves as a cornerstone in unraveling the complexities of IL-6 signaling, shedding light on its roles in health and disease. Its applications span from fundamental research to therapeutic development, showcasing its potential to shape the future of precision medicine.

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.

Description:

Twisted Gastrulation Protein Human Recombinant

Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.

Product # :

CYT-873

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Description

TWSG1 Human Recombinant (26-223) produced in CHO is a single, glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass ranging from 35-43kDa on SDS-PAGE due to glycosylation.The TWSG1 is purified by proprietary chromatographic techniques.

Source

CHO.

Formulation

Lyophilized from a 0.2µm filtered solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured by its ability to inhibit alkaline phosphatase production induced by rHuBMP-6 in mouse ATDC5 cells, is less than 16µg/ml.

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Introduction
Twisted gastrulation Protein (TSG) is a secreted, cysteine-rich protein which has a role in dorsal/ventral patterning in Drosophila and Xenopus by regulating BMP signaling. TSG functions as an agonist for BMP signaling by controlling the inhibitory actions of the BMP antagonist, Chordin/Sog, and the cleavage properties of the metalloprotease, xolloid/tolloid. TSG N-terminal domain binds BMP protein directly and displays BMP antagonist activity.
Synonyms
Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSG 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 TSG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CNKALCASDV SKCLIQELCQ CRPGEGNCSC CKECMLCLGA LWDECCDCVG MCNPRNYSDT PPTSKSTVEE LHEPIPSLFR ALTEGDTQLN WNIVSFPVAE ELSHHENLVS FLETVNQPHH QNVSVPSNNV HAPYSSDKEH MCTVVYFDDC MSIHQCKISC ESMGASKYRW FHNACCECIG PECIDYGSKT VKCMN CMF.

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.

Description:

Leptin Chicken Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-505

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Description

Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 95.0% 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. Its activity is however 5-10 fold lower as compared to mammalian leptins.

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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 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 Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Cys-Gln.
Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.

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

Description:

Leptin Horse Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-504

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Description

Leptin Horse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 95.0% 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.

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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 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 Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.1 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Horse as a Reference Standard.

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

Description:

Yersinia Enterocolitica (O:9) YopE Recombinant

Outer membrane virulence protein YopE, yopE, yop25.

Product # :

PRO-2576

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Description

Recombinant Yersinia Enterocolitica (O:9) YopE in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 24kDa. Y.Enterocolitica (O:9) YopE is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Y.Enterocolitica (O:9) YopE is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
A main factor of pathogenic Yersinia enterocolitica strains is a plasmid-encoded type 3 secretion system, through which Yersinia outer proteins (Yops) are injected into the host cell. Yop E is a GTPase activation protein which controls pore formation by activating small Rho GTPase, causing inhibition of actin polymerization.
Synonyms
Outer membrane virulence protein YopE, yopE, yop25.
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 Activity
Binds IgG- and IgM-type human antibodies.

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.

Description:

Insulin Like Growth Factor-1, Mutant R36Q Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-1090

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Description

IGF1 R36Q Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa. The IGF1 R36Q is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 R36Q Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM PB and 150 mM NaCl, pH 5.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
Solubility
It is recommended to reconstitute the lyophilized IGF1 R36Q in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSQRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
Background
What is the molecular weight/Mw of IGF1 HUMAN, R36Q Protein?
IGF1 HUMAN, R36Q Protein has a total Mw of 7.7kDa.

What is the source or expression system of IGF1 HUMAN, R36Q Protein?
Escherichia Coli.

What is the Purity of IGF1 HUMAN, R36Q Protein?
IGF1 HUMAN, R36Q Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 HUMAN, R36Q Protein?
The biological functionality of IGF1 HUMAN, R36Q Protein will be determined in the future.

What is the amino acid sequence of IGF1 HUMAN, R36Q Protein?
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSQRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

What applications can IGF1 HUMAN, R36Q Protein be used in?
IGF1 HUMAN, R36Q Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 HUMAN, R36Q Protein?
The endotoxin level is minimal, IGF1 HUMAN, R36Q 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.

Description:

Complement C3 Rat

Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

Product # :

PRO-2706

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Description

Rat Complement C3 produced in Rat plasma having a molecular weight of 187kDa.

Source

Rat Plasma.

Formulation

C3 solution contains phosphate buffer saline.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
C3 is central to the activation of all 3 pathways of complement activation. Initiation of each pathway generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3 activated during complement activation never attaches to the surface due to its thioester reaction with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all 3 pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane.
Synonyms
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Physical Appearance
Sterile filtered solution.
Stability
C3 Mouse 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.

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.

Description:

Complement C3b Inactivated Mouse

Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

Product # :

PRO-2813

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Description

Mouse Complement C3b Inactivated produced in Mouse serum having a molecular weight of 175kDa.

Source

Mouse serum.

Formulation

C3b Mouse Inactivated solution contains PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Physical Appearance
Sterile Filtered solution.
Stability
C3b Mouse Inactivated 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.
Background
Complement component 3b (C3b) is a key protein in the complement system, a crucial component of the innate immune response. C3b plays a pivotal role in opsonization, inflammation, and clearance of pathogens and damaged cells. In mouse models, research on C3b has provided valuable insights into its mechanism of action, activity, and implications in immune function. This paper aims to delve into the dynamics of mouse C3b, shedding light on its functional attributes and potential applications in immunological research. C3b Inactivated protein has lost its biological capabilities due to structural changes compared to C3b that has binding sites to factor P, factor H, factor B, factorC5, and factor-I and therefore it destroys these sites.
Significantly, C3b inactivated protein cannot bind factor B and is therefore it cannot participate in complement activation.
C3b inactivated protein still binds tC50 properdin and CR3 receptor.

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.

Description:

SARS MERS Spike S2 Recombinant

Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERSCoV S2 P, Spike2 glycoprotein, S2 glycoprotein, S2, Spike S2 Subunit protein, S2 Subunit

Product # :

SARS-053

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Description

SARS MERS S2 Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 554 amino acids (752-1296aa) and having a molecular mass of 60.7kDa.SARS MERS S2 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The SARS MERS S2 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.
Synonyms
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERSCoV S2 P, Spike2 glycoprotein, S2 glycoprotein, S2, Spike S2 Subunit protein, S2 Subunit
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
ADPSVPGEMR LASIAFNHPI QVDQLNSSYF KLSIPTNFSF GVTQEYIQTT IQKVTVDCKQ YVCNGFQKCE QLLREYGQFC SKINQALHGA NLRQDDSVRN LFASVKSSQS SPIIPGFGGD FNLTLLEPVS ISTGSRSARS AIEDLLFDKV TIADPGYMQG YDDCMQQGPA SARDLICAQY VAGYKVLPPL MDVNMEAAYT SSLLGSIAGV GWTAGLSSFA AIPFAQSIFY RLNGVGITQQ VLSENQKLIA NKFNQALGAM QTGFTTTNEA FQKVQDAVNN NAQALSKLAS ELSNTFGAIS ASIGDIIQRL DVLEQDAQID RLINGRLTTL NAFVAQQLVR SESAALSAQL AKDKVNECVK AQSKRSGFCG QGTHIVSFVV NAPNGLYFMH VGYYPSNHIE VVSAYGLCDA ANPTNCIAPV NGYFIKTNNT RIVDEWSYTG SSFYAPEPIT SLNTKYVAPQ VTYQNISTNL PPPLLGNSTG IDFQDELDEF FKNVSTSIPN FGSLTQINTT LLDLTYEMLS LQQVVKALNE SYIDLKELGN YTYYNKWPHH HHHH

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.

Description:

SARS MERS Spike Recombinant

Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein

Product # :

SARS-051

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Description

SARS MERS Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1285 amino acids (18-1296aa) and having a molecular mass of 141.6kDa.SARS MERS is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The SARS MERS solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.
Synonyms
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein
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
YVDVGPDSVK SACIEVDIQQ TFFDKTWPRP IDVSKADGII YPQGRTYSNI TITYQGLFPY QGDHGDMYVY SAGHATGTTP QKLFVANYSQ DVKQFANGFV VRIGAAANST GTVIISPSTS ATIRKIYPAF MLGSSVGNFS DGKMGRFFNH TLVLLPDGCG TLLRAFYCIL EPRSGNHCPA GNSYTSFATY HTPATDCSDG NYNRNASLNS FKEYFNLRNC TFMYTYNITE DEILEWFGIT QTAQGVHLFS SRYVDLYGGN MFQFATLPVY DTIKYYSIIP HSIRSIQSDR KAWAAFYVYK LQPLTFLLDF SVDGYIRRAI DCGFNDLSQL HCSYESFDVE SGVYSVSSFE AKPSGSVVEQ AEGVECDFSP LLSGTPPQVY NFKRLVFTNC NYNLTKLLSL FSVNDFTCSQ ISPAAIASNC YSSLILDYFS YPLSMKSDLS VSSAGPISQF NYKQSFSNPT CLILATVPHN LTTITKPLKY SYINKCSRLL SDDRTEVPQL VNANQYSPCV SIVPSTVWED GDYYRKQLSP LEGGGWLVAS GSTVAMTEQL QMGFGITVQY GTDTNSVCPK LEFANDTKIA SQLGNCVEYS LYGVSGRGVF QNCTAVGVRQ QRFVYDAYQN LVGYYSDDGN YYCLRACVSV PVSVIYDKET KTHATLFGSV ACEHISSTMS QYSRSTRSML KRRDSTYGPL QTPVGCVLGL VNSSLFVEDC KLPLGQSLCA LPDTPSTLTP RSVRSVPGEM RLASIAFNHP IQVDQLNSSY FKLSIPTNFS FGVTQEYIQT TIQKVTVDCK QYVCNGFQKC EQLLREYGQF CSKINQALHG ANLRQDDSVR NLFASVKSSQ SSPIIPGFGG DFNLTLLEPV SISTGSRSAR SAIEDLLFDK VTIADPGYMQ GYDDCMQQGP ASARDLICAQ YVAGYKVLPP LMDVNMEAAY TSSLLGSIAG VGWTAGLSSF AAIPFAQSIF YRLNGVGITQ QVLSENQKLI ANKFNQALGA MQTGFTTTNE AFQKVQDAVN NNAQALSKLA SELSNTFGAI SASIGDIIQR LDVLEQDAQI DRLINGRLTT LNAFVAQQLV RSESAALSAQ LAKDKVNECV KAQSKRSGFC GQGTHIVSFV VNAPNGLYFM HVGYYPSNHI EVVSAYGLCD AANPTNCIAP VNGYFIKTNN TRIVDEWSYT GSSFYAPEPI TSLNTKYVAP QVTYQNISTN LPPPLLGNST GIDFQDELDE FFKNVSTSIP NFGSLTQINT TLLDLTYEML SLQQVVKALN ESYIDLKELG NYTYYNKWPH HHHHH

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.

Description:

Insulin Like Growth Factor-1, Mutant V44M Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-1088

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Quantity :

Shipping Method :

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Description

IGF1 V44M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa. The IGF1 V44M is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 V44M Lyophilized from a 0.2 µm filtered concentrated solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
Solubility
It is recommended to reconstitute the lyophilized IGF1 V44M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIMDECCFR SCDLRRLEMY
CAPLKPAKSA
Background
What is the molecular weight/Mw of IGF1 HUMAN, V44M Protein?
IGF1 HUMAN, V44M Protein has a total Mw of 7.7kDa.

What is the source or expression system of IGF1 HUMAN, V44M Protein?
Escherichia Coli.

What is the Purity of IGF1 HUMAN, V44M Protein?
IGF1 HUMAN, V44M Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 HUMAN, V44M Protein?
The biological functionality of IGF1 HUMAN, V44M Protein will be determined in the future.

What is the amino acid sequence of IGF1 HUMAN, V44M Protein?
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIMDECCFR SCDLRRLEMY.

What applications can IGF1 HUMAN, V44M Protein be used in?
IGF1 HUMAN, V44M Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 HUMAN, V44M Protein?
The endotoxin level is minimal, IGF1 HUMAN, V44M 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.

Description:

Adiponectin Mouse Recombinant, HEK

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-435

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Quantity :

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formulation
purity
biological activity
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Description

The Acrp30 Mouse Recombinant is fused with FLAG tag having a total Mw of 26kDa.

Source

HEK293 (Human embryonic kidney cell line).

Formulation

Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M PBS buffer,0.075M NaCl, pH7.4.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.

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Introduction
Adiponectin is an important negative regulator in hematopoiesis and immune systems. It may be involved in ending inflammatory responses through its inhibitory functions. Inhibits endothelial nf-kappa-b signaling through a camp-dependent pathway. Inhibits tnf-alpha- induced expression of endothelial adhesion molecules. Involved in the control of fat metabolism and insulin sensitivity.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Stability
Store lyophilized APM-1 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 reconstitute the lyophilized Acrp30 Mouse in sterile 18M-cm H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293.

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

What is the Biological Activity of ADIPONECTIN Protein?
Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.

What is the amino acid sequence of ADIPONECTIN Protein?
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.

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.

Description:

Myo-Inositol Oxygenase Human Recombinant

Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.

Product # :

ENZ-812

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

MIOX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Trp285) containing 295 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 34.2kDa.

Source

Escherichia Coli.

Formulation

MIOX was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl and 5% (w/v) trehalose, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Inositol oxygenase is a non-heme di-iron enzyme which oxidizes myo-inositol to glucuronic acid. In addition, inositol oxygenase oxidizes the less abundant chiro isomer of inositol. MIOX enzyme is a component of the only known pathway for the catabolism of inositol in humans. MIOX is expressed mostly in the kidneys. Reduction of Inositol Oxygenase and accumulation of polyols, such as inositol and xylitol, have been implicated as contributing factors in complications linked with diabetes.
Synonyms
Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.
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. MIOX is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASMKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW.

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.

Description:

mRNA Turnover 4 Human Recombinant

MRNA Turnover 4 Homolog (S. Cerevisiae), MRT4 MRNA Turnover 4 Homolog (S. Cerevisiae), 60S Acidic Ribosomal Protein PO, Chromosome 1 Open Reading Frame 33, C1orf33, MRT4, DJ657E11.4.

Product # :

PRO-1233

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source
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Description

MRTO4 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (1-239) and having a molecular mass of 29.9 kDa.MRTO4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The MRTO4 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
mRNA turnover protein 4 homolog (MRTO4) is a member of the ribosomal protein L10P family. MRTO4 is a protein sharing a low level of sequence similarity with ribosomal protein P0. Though the precise function of the MRTO4 is presently unknown, it seems to be involved in mRNA turnover and ribosome assembly. MRTO4 is a nucleolar component of the ribosome assembly apparatus which shares remarkable similarity and contends for binding to the 25S rRNA GAR domain with the ribosomal protein P0. The MRTO4 gene is located on human chromosome 1, which extends over 260 million base pairs, is comprised of over 3,000 genes and contains approximately 8% of the human genome.
Synonyms
MRNA Turnover 4 Homolog (S. Cerevisiae), MRT4 MRNA Turnover 4 Homolog (S. Cerevisiae), 60S Acidic Ribosomal Protein PO, Chromosome 1 Open Reading Frame 33, C1orf33, MRT4, DJ657E11.4.
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 MGSMPKSKRD KKVSLTKTAK KGLELKQNLI EELRKCVDTY KYLFIFSVAN MRNSKLKDIR NAWKHSRMFF GKNKVMMVAL GRSPSDEYKD NLHQVSKRLR GEVGLLFTNR TKEEVNEWFT KYTEMDYARA GNKAAFTVSL DPGPLEQFPH SMEPQLRQLG LPTALKRGVV TLLSDYEVCK EGDVLTPEQA RVLKLFGYEM AEFKVTIKYM WDSQSGRFQQ MGDDLPESAS ESTEESDSED DD

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.

Description:

Small Nuclear Ribonucleoprotein Polypeptide B Human Recombinant

Small nuclear ribonucleoprotein polypeptide B2, Msl1, U2 snRNP B'', U2 small nuclear ribonucleoprotein B'', MGC24807, MGC45309.

Product # :

PRO-217

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Quantity :

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Description

SNRPB2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-225a.a.) and having a molecular mass of 27.6kDa. The SNRPB2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SNRPB2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SNRPB2 is a member of the RRM U1 A/B family. SNRPB2 links with stem loop IV of U2 small nuclear ribonucleoprotein (U2 snRNP) in the presence of snRNP-A. SNRPB2 has a part in pre-mRNA splicing. Autoantibodies from patients with systemic lupus erythematosus often identify epitopes on the encoded protein. A pair of transcript variants encoding the same protein were identified for this gene.
Synonyms
Small nuclear ribonucleoprotein polypeptide B2, Msl1, U2 snRNP B'', U2 small nuclear ribonucleoprotein B'', MGC24807, MGC45309.
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 MDIRPNHTIY INNMNDKIKK EELKRSLYAL FSQFGHVVDI VALKTMKMRG QAFVIFKELG SSTNALRQLQ GFPFYGKPMR IQYAKTDSDI ISKMRGTFAD KEKKKEKKKA KTVEQTATTT NKKPGQGTPN SANTQGNSTP NPQVPDYPPN YILFLNNLPE ETNEMMLSML FNQFPGFKEV RLVPGRHDIA FVEFENDGQA GAARDALQGF KITPSHAMKI TYAKK

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.

Description:

Advanced Glycosylation End Product-Specific Receptor Human Recombinant

Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.

Product # :

PRO-600

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

sRAGE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 339 amino acids and having a molecular mass of 36.5 kDa. The Human sRAGE is fused to a 14 a.a. His tag at N-Terminus.The Human sRAGE is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile filtered (0.4 µm) concentrated (0.5mg/ml) protein solution was lyophilized with 30mM acetate buffer pH-4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
sRAGE is a member of the immunoglobulin superfamily of cell surface molecules. sRAGE is a receptor for various molecules, including the amyloidogenic form of serum amyloid A, amyloid-beta protein, members of the S100/calgranulin superfamily and advanced glycation end products. sRAGE lies within the major histocompatibility complex (MHC) class III region on chromosome 6. Alternative splicing results in two transcript variants encoding different isoforms. sRAGE mediates interactions of nonenzymatic glycosylated proteins which accumulate in vascular tissue during aging & at an increasing rate in diabetes. sRAGE is a receptor for amyloid beta peptide.
Synonyms
Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.
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 0.1M Acetate buffer pH4 to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MRGSHHHHHH GMASAQNITA RIGEPLVLKC KGAPKKPPQR LEWKLNTGRT EAWKVLSPQG GGPWDSVARV LPNGSLFLPAV GIQDEGIFRCQ AMNRNGKETKS NYRVRVYQIP GKPEIVDSASE LTAGVPNKVG TCVSEGSYPA GTLSWHLDGKPL VPNEKGVSVK EQTRRHPETG LFTLQSELMV TPARGGDPRP TFSCSFSPGL PRHRALRTAP IQPRVWEPVPL EEVQLVVEPE GGAVAPGGTV TLTCEVPAQP SPQIHWMKDGVP LPLPPSPVLI LPEIGPQDQG TYSCVATHSS HGPQESRAVS ISIIEPGEEG PTAGEGFDKV REAEDSPQHM

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.

Description:

Borrelia Miyamotoi GlpQ Recombinant

Product # :

BOR-022

Price :

Quantity :

Shipping Method :

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source
formulation
purity
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Description

Recombinant Borrelia Miyamotoi GlpQ produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 38,132 Dalton. Borrelia Miyamotoi GlpQ is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Borrelia Miyamotoi GlpQ is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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.

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.

Description:

Galectin-7 Human Recombinant

Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.

Product # :

CYT-016

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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purity
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Description

Galectin-7 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 136 amino acids and having a molecular mass of 15kDa.The LGALS7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LGALS7 was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris, 150mM NaCl, 1mM EDTA and 5% Trehalose, pH 8.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.
Synonyms
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LGALS7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-7 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Galectin-7 in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNP
RLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQ
YHHFRHRLPLARVRLVEVGGDVQLDSVRIF
Background
What is the molecular weight/Mw of LGALS7 HUMAN Protein?
LGALS7 HUMAN Protein has a total Mw of 15kDa.

What is the source or expression system of LGALS7 HUMAN Protein?
Escherichia Coli.

What is the Purity of LGALS7 HUMAN Protein?
LGALS7 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS7 HUMAN Protein?
The biological functionality of LGALS7 HUMAN Protein will be determined in the future.

What is the amino acid sequence of LGALS7 HUMAN Protein?
MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNP
RLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQ
YHHFRHRLPLARVRLVEVGGDVQLDSVRIF

What applications can LGALS7 HUMAN Protein be used in?
LGALS7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS7 HUMAN Protein?
The endotoxin level is minimal, LGALS7 HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Ubiquitin-Like Domain Containing CTD Phosphatase 1 Human Recombinant

CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.

Product # :

PRO-151

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Description

UBLCP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 39.2kDa.UBLCP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

UBLCP1 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation averts assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.
Synonyms
CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.
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 MGSMALPIIV KWGGQEYSVT TLSEDDTVLD LKQFLKTLTG VLPERQKLLG LKVKGKPAEN DVKLGALKLK PNTKIMMMGT REESLEDVLG PPPDNDDVVN DFDIEDEVVE VENREENLLK ISRRVKEYKV EILNPPREGK KLLVLDVDYT LFDHRSCAET GVELMRPYLH EFLTSAYEDY DIVIWSATNM KWIEAKMKEL GVSTNANYKI TFMLDSAAMI TVHTPRRGLI DVKPLGVIWG KFSEFYSKKN TIMFDDIGRN FLMNPQNGLK IRPFMKAHLN RDKDKELLKL TQYLKEIAKL DDFLDLNHKY WERYLSKKQG Q.

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.

Description:

Cytokine-Like 1 Human Recombinant

Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.

Product # :

CYT-775

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

CYTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 23-136) containing 124 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 14.6kDa (calculated).

Source

Escherichia Coli.

Formulation

CYTL1 was filtered (0.4 µm) 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.

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Introduction
Cytokine-like protein 1 (CYTL1) is a secreted protein. CYTL1 is expressed in CD34+ cell populations of bone marrow and cord blood which function as hematopoietic stem/progenitor cells. However, CYTL1 is not expressed in CD34- cells. Experiments with knock-out mice (Cytl1-/-) propose that CYTL1 is essential for the maintenance of cartilage homeostasis rather than cartilage and bone development, and loss of CYTL1 function is linked with experimental osteoarthritic cartilage destruction in mice.
Synonyms
Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. CYTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.
Background
Title: Cytokine-Like 1 Human Recombinant: Exploring its Role in Immune Regulation and Therapeutic Potential
Abstract:

Cytokine-like 1 (CYTL1) is an emerging cytokine that exhibits pleiotropic effects on immune regulation and tissue homeostasis. This research paper provides a comprehensive analysis of human recombinant CYTL1, focusing on its production, characterization, and potential applications in immune modulation. The paper highlights the significance of CYTL1 in immune cell function, inflammation, and tissue repair. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYTL1 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYTL1 and its utility as a research tool and a potential immunotherapeutic agent.
Introduction:

Cytokine-like 1 (CYTL1) is a recently discovered cytokine with diverse biological functions, including immune regulation and tissue repair. Human recombinant CYTL1, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological activities and explore its therapeutic potential.
Production and Characterization:

Recombinant CYTL1 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYTL1.
Role in Immune Regulation:

CYTL1 has been shown to modulate immune cell function and inflammation. It can influence the differentiation and activation of various immune cell subsets, including T cells and macrophages. Recombinant CYTL1 serves as a valuable tool for investigating the mechanisms underlying immune regulation and exploring its potential as an immunomodulatory agent.
Therapeutic Implications:

The dysregulation of immune responses is associated with numerous pathological conditions, including autoimmune diseases and chronic inflammation. Recombinant CYTL1 holds promise as a potential immunotherapeutic agent due to its ability to modulate immune cell function and regulate inflammatory processes. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYTL1 in various diseases, including autoimmune disorders and tissue regeneration.
Conclusion:

Human recombinant CYTL1 is a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune regulation contribute to our understanding of immune responses and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYTL1 offer promising avenues for improving outcomes in autoimmune diseases, chronic inflammation, and tissue repair.
What is the molecular weight/Mw of CYTL1 Protein?
CYTL1 Protein has a total Mw of 14.6kDa.

What is the source or expression system of CYTL1 Protein?
Escherichia Coli.

What is the Purity of CYTL1 Protein?
CYTL1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CYTL1 Protein?
The biological functionality of CYTL1 Protein will be determined in the future.

What is the amino acid sequence of CYTL1 Protein?
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.

What applications can CYTL1 Protein be used in?
CYTL1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CYTL1 Protein?
The endotoxin level is minimal, CYTL1 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.

Description:

Speckle-Type POZ Protein Human Recombinant

Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

Product # :

PRO-195

Price :

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Shipped with Ice Packs

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Description

SPOP Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 394 amino acids (1-374 a.a.) and having a molecular mass of 44.3kDa. The SPOP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SPOP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 0.2M NaCl and 2mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Speckle-type POZ protein (SPOP) belongs to the Tdpoz family containing one N-terminal MATH (Meprin and TRAF homology) domain and one C-terminal BTB/POZ domain. SPOP inhibits IPF1/PDX1 transactivation of established target promoters, may be by recruiting a repressor complex. SPOP is involved in ubiquitinylation and protein degradation as a result of an interaction with CUL-3.
Synonyms
Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.
Physical Appearance
SPOP is supplied as a 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 MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE
VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ CPFLGPPRKR LKQS.

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.

Description:

Oncostatin-M Mouse Recombinant

Oncostatin-M, OSM, OncoM.

Product # :

CYT-168

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

OSM Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.4kDa.The OSM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

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 the dose-dependent stimulation of the proliferation of NIH-3T3 mouse embryonic fibroblast cells is < 1 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
Synonyms
Oncostatin-M, OSM, OncoM.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NRGCSNSSSQ LLSQLQNQAN LTGNTESLLE PYIRLQNLNT PDLRAACTQH SVAFPSEDTL RQLSKPHFLS TVYTTLDRVL YQLDALRQKF LKTPAFPKLD SARHNILGIR NNVFCMARLL NHSLEIPEPT QTDSGASRST TTPDVFNTKI GSCGFLWGYH RFMGSVGRVF REWDDGSTRS R.

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

Description:

Betacellulin Human Recombinant, His Tag

Betacellulin, Probetacellulin.

Product # :

CYT-077

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Shipped with Ice Packs

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sds-page

Description

BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
Synonyms
Betacellulin, Probetacellulin.
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 MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 11.3kDa.

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

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

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

What is the amino acid sequence of BETACELLULIN Protein?
MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

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

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

Description:

Glia Maturation Factor Beta Human Recombinant

Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

Product # :

CYT-565

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Glia Maturation Factor-Beta (GMF-Beta) Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.5 kDa. Glia Maturation Factor-Beta, GMF-Beta, Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GMF-beta protein was lyophilized after dialysis against 20mM PBS pH=7.4 and 130mM NaCl.

Purity

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

More Info

Introduction
Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.
Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMF-B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMF-beta should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GMFB in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.
Background
What is the molecular weight/Mw of GMFB HUMAN Protein?
GMFB HUMAN Protein has a total Mw of 16.5kDa.

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

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

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

What is the amino acid sequence of GMFB HUMAN Protein?
SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.

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

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

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

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