Spike Protein

SARS-COV-2-RBD (P0DTC2.1)

SARS-CoV-2 is a member of the betacoronavirus genus and is closely related to SARS-CoV (Wrapp et al. 2020). In general, three structural proteins are associated with the viral envelope of corona viruses: a membrane protein (M), an envelope protein (E) and a spike protein (S). The spike protein consists of three segments: an ectodomain (including subunits S1 and S2), a transmembrane anchor and a short intracellular tail. The trimeric transmembrane spike glycoprotein (S) mediates the coronavirus entry by receptor binding and membrane fusion. It consists of two functional subunits named S1 and S2. S1 mediates binding to the host receptor and shows a high diversity among corona viruses. S2 induces fusion of the virus with the cellular membrane of the host and is conserved.

S is synthesized as a single-chain precursor and trimerizes upon folding. Corona virus S proteins include up to two protease cleavage sites, i.e. between the S1 and S2 subunits (S1/S2) and upstream of the fusion peptide (S2’) (Walls et al. 2017). To bind a host cell receptor, the receptor-binding domain (RBD) of S1 has do undergo hinge-like conformational movements resulting in hiding or exposing the determinants of receptor binding. SARS-CoV-2 RBD consist of 223 amino acids (Lan et al. 2020). Nine cysteine residues are found within the RBD resulting in four disulfide bonds. RBM is described as receptor binding motif containing most of the residues that bind to ACE2.

SARS-CoV-2 spike RBD proteins – AVAILABLE NOW!

Sample Quantity and Formulation

Lyophilized protein preparation or protein solution.

Secreted crude protein from Komagataella phaffii (Pichia pastoris) strain BSYBG11 (cell free), lyophilized or in a solution (10 mM KH2PO4/K2HPO4 at pH 7.4). Constructs with polyhistidine-tag are Ni-NTA purified. All constructs are also available without tag.

Price: 200,- € per 1 mg

 

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Prices do not include VAT, additional taxes or fees might apply. Shipping fees will be charged. Products are for research only. No resale of products.

SARS-CoV-2 RBD customized proteins

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Click on Protein Product below and view SDS-PAGE and/or Western blot of SARS-CoV-2 RBD-(variants) expressed in P. pastoris.

SARS-CoV-2 RBD is expressed as glycosylated protein ranging in size between 45-55 kDa. After digestion with PNGase F the protein appears just above 25 kDa correlating with its calculated molecular weight. Hyper-glycosylation is largely prevented in variant RBD-T3, while at the same time maintaining expressibility. Variants without glycosylation sites (RBD-N1 and -T1) were found smaller than calculated, however still able to bind the applied polyclonal spike RBD antibody.

 

Protein Product

RBD

SARS-CoV-2 RBD wild type

(C-term 6xHis, Ni-NTA purified)

 

SDS-PAGE reduced and denatured. 

RBD-M81

SARS-CoV-2 RBD wild type produced in strain BSY10M81

(C-term 6xHis, Ni-NTA purified)

 

SDS-PAGE reduced and denatured. 

RBD-T3

Glycoengineered variant

(C-term 6xHis, Ni-NTA purified)

 

SDS-PAGE reduced and denatured. 

RBD-T3-M81

Glycoengineered variant produced in strain BSY10M81

(C-term 6xHis, Ni-NTA purified)

 

SDS-PAGE reduced and denatured. 

RBD-RAD

Mutation in integrin binding site (RGD > RAD)

 

Western blot, primary antibody SARS-CoV-2 Spike RBD Antibody, Rabbit PAb (Sino Inc.). 

RBD-N1

Glycoengineered variant

 

Western blot, primary antibody SARS-CoV-2 Spike RBD Antibody, Rabbit PAb (Sino Inc.). 

RBD-T1

Glycoengineered variant

also available with C-term 6xHis

 

Western blot, primary antibody SARS-CoV-2 Spike RBD Antibody, Rabbit PAb (Sino Inc.). 

HSA-RBD

N-terminal fusion to human serum albumin

 

Western blot, primary antibody SARS-CoV-2 Spike RBD Antibody, Rabbit PAb (Sino Inc.). 

HSA-T3

N-terminal fusion to human serum albumin

 

Western blot, primary antibody SARS-CoV-2 Spike RBD Antibody, Rabbit PAb (Sino Inc.). 

Gene Sequence

R
319
V
320
Q
321
P
322
T
323
E
324
S
325
I
326
V
327
R
328
F
329
P
330
N
331
I
332
T
333
N
334
L
335
C
336
P
337
F
338
G
339
E
340
V
341
F
342
N
343
A
344
T
345
R
346
F
347
A
348
S
349
V
350
Y
351
A
352
W
353
N
354
R
355
K
356
R
357
I
358
S
359
N
360
C
361
V
362
A
363
D
364
Y
365
S
366
V
367
L
368
Y
369
N
370
S
371
A
372
S
373
F
374
S
375
T
376
F
377
K
378
C
379
Y
380
G
381
V
382
S
383
P
384
T
385
K
386
L
387
N
388
D
389
L
390
C
391
F
392
T
393
N
394
V
395
Y
396
A
397
D
398
S
399
F
400
V
401
I
402
R
403
G
404
D
405
E
406
V
407
R
408
Q
409
I
410
A
411
P
412
G
413
Q
414
T
415
G
416
K
417
I
418
A
419
D
420
Y
421
N
422
Y
423
K
424
L
425
P
426
D
427
D
428
F
429
T
430
G
431
C
432
V
433
I
434
A
435
W
436
N
437
S
438
N
439
N
440
L
441
D
442
S
443
K
444
V
445
G
446
G
447
N
448
Y
449
N
450
Y
451
L
452
Y
453
R
454
L
455
F
456
R
457
K
458
S
459
N
460
L
461
K
462
P
463
F
464
E
465
R
466
D
467
I
468
S
469
T
470
E
471
I
472
Y
473
Q
474
A
475
G
476
S
477
T
478
P
479
C
480
N
481
G
482
V
483
E
484
G
485
F
486
N
487
C
488
Y
489
F
490
P
491
L
492
Q
493
S
494
Y
495
G
496
F
497
Q
498
P
499
T
500
N
501
G
502
V
503
G
504
Y
505
Q
506
P
507
Y
508
R
509
V
510
V
511
V
512
L
513
S
514
F
515
E
516
L
517
L
518
H
519
A
520
P
521
A
522
T
523
V
524
C
525
G
526
P
527
K
528
K
529
S
530
T
531
N
532
L
533
V
534
K
535
N
536
K
537
C
538
V
539
N
540
F
541

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    References

    Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., … McLellan, J. S. (2020). Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation. BioRxiv : The Preprint Server for Biology. https://doi.org/10.1101/2020.02.11.944462

    Walls, A. C., Park, Y. J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020). Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell, 181(2), 281-292.e6. https://doi.org/10.1016/j.cell.2020.02.058

    Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., … Wang, X. (2020). Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature, 581(7807), 215–220. https://doi.org/10.1038/s41586-020-2180-5